[{"title":"Research data for \"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants\"","publisher":"Institute of Science and Technology Austria","_id":"21284","OA_place":"repository","date_published":"2026-02-18T00:00:00Z","oa":1,"month":"2","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","image":"/images/cc_by_nc.png","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"corr_author":"1","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","citation":{"ama":"Becker LM, Schanda P. Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21284\">10.15479/AT-ISTA-21284</a>","short":"L.M. Becker, P. Schanda, (2026).","ista":"Becker LM, Schanda P. 2026. Research data for ‘Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-21284\">10.15479/AT-ISTA-21284</a>.","ieee":"L. M. Becker and P. Schanda, “Research data for ‘Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.’” Institute of Science and Technology Austria, 2026.","chicago":"Becker, Lea Marie, and Paul Schanda. “Research Data for ‘Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.’” Institute of Science and Technology Austria, 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-21284\">https://doi.org/10.15479/AT-ISTA-21284</a>.","apa":"Becker, L. M., &#38; Schanda, P. (2026). Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-21284\">https://doi.org/10.15479/AT-ISTA-21284</a>","mla":"Becker, Lea Marie, and Paul Schanda. <i>Research Data for “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.”</i> Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21284\">10.15479/AT-ISTA-21284</a>."},"doi":"10.15479/AT-ISTA-21284","article_processing_charge":"No","date_created":"2026-02-17T10:17:14Z","oa_version":"Published Version","file_date_updated":"2026-02-17T10:11:14Z","abstract":[{"lang":"eng","text":"The advantageous characteristics attributed to the 19F nucleus have made it a popular target for NMR once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle-spinning NMR to fluorine-labeled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilized to get structural insights into proteins and measure long distances. Despite increasing popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR often suffers from slow longitudinal T1 relaxation and therefore long recycle delays. In this work, we expand paramagnetic doping, an approach commonly used to reduce proton T1 relaxation times, to 19F-labeled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F and 13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labeled protein via 19F-detected MAS NMR experiments. The observed paramagnetic relaxation enhancement substantially reduces measurement times of 19F MAS NMR experiments without compromising resolution. Additionally, we report the chemical-shift assignments of all four fluorotryptophan signals in the 12 × 39 kDa large protein using a mutagenesis approach."}],"author":[{"last_name":"Becker","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie","first_name":"Lea Marie"},{"full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda"}],"ddc":["541"],"contributor":[{"last_name":"Toscano","contributor_type":"researcher","first_name":"Giorgia","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4"},{"id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna","contributor_type":"researcher","last_name":"Kapitonova"},{"last_name":"Singh","contributor_type":"researcher","first_name":"Rajkumar","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20"},{"id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","first_name":"Undina","contributor_type":"researcher","last_name":"Guillerm"},{"first_name":"Roman","last_name":"Lichtenecker","contributor_type":"researcher"}],"fulldoi":"https://doi.org/10.15479/AT-ISTA-21284","day":"18","date_updated":"2026-06-10T09:28:41Z","has_accepted_license":"1","status":"public","license":"https://creativecommons.org/licenses/by-nc/4.0/","type":"research_data","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"file":[{"access_level":"open_access","date_created":"2026-02-17T10:11:14Z","file_id":"21285","checksum":"2d3105f26be578073b88ee1f2ea0bdb1","file_size":36996027,"success":1,"creator":"lbecker","content_type":"application/zip","file_name":"Research_data.zip","relation":"main_file","date_updated":"2026-02-17T10:11:14Z"},{"date_updated":"2026-02-17T10:11:14Z","creator":"lbecker","content_type":"text/plain","file_name":"README.txt","relation":"table_of_contents","date_created":"2026-02-17T10:11:14Z","access_level":"open_access","file_id":"21286","checksum":"e24aebcdb8856cb181cbaa02de020ddb","file_size":1993}],"year":"2026","OA_type":"free access","acknowledgement":"We thank Ben P. Tatman for insightful discussions. This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility."},{"type":"journal_article","status":"public","has_accepted_license":"1","project":[{"name":"Structure and mechanism of the mitochondrial MIM insertase","grant_number":"I06223","_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0"}],"issue":"6","day":"01","date_updated":"2026-06-02T07:26:34Z","fulldoi":"https://doi.org/10.1002/pro.70630","pmid":1,"scopus_import":"1","ddc":["572"],"acknowledgement":"We gratefully acknowledge research funding by the Austrian Science Fund (FWF), projects 10.55776/PAT1647625 and 10.55776/I6223. We thank Prof. Long Li (Peking University) for providing structural models and EM density for the TOM and TIM23 complexes, used to generate part of Figure 3. Open Access funding provided by Institute of Science and Technology Austria.","quality_controlled":"1","OA_type":"hybrid","year":"2026","file":[{"date_updated":"2026-06-02T07:23:12Z","content_type":"application/pdf","relation":"main_file","file_name":"2026_ProteinScience_Schneider.pdf","creator":"dernst","success":1,"file_size":3897305,"file_id":"21937","date_created":"2026-06-02T07:23:12Z","access_level":"open_access","checksum":"e0163459a7238fdcc3fc5e17bedcce9a"}],"PlanS_conform":"1","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"volume":35,"month":"06","oa":1,"OA_place":"publisher","date_published":"2026-06-01T00:00:00Z","_id":"21929","publisher":"Wiley","article_type":"original","title":"Dynamic disorder is crucial for mitochondrial protein import","external_id":{"pmid":["42159315"]},"abstract":[{"text":"The import of proteins into mitochondria poses fundamental mechanistic challenges: aggregation-prone precursor proteins must be maintained in aqueous compartments and threaded through narrow pores without becoming stuck or mislocalized. Recent evidence from mitochondrial protein import studies and other chaperone systems underscores the critical role of dynamics in balancing sufficiently tight binding, promiscuity, specificity, and release. Dynamic binding of client precursor proteins to import machinery components arises naturally from the avidity of their interactions. Conformational entropy enhances their stability, while the multivalent nature of these interactions ensures that client transfer to downstream insertases occurs without a substantial energy barrier. Here, we discuss this emerging paradigm of dynamic protein handling, using examples where dynamic structures have been resolved and highlight outstanding questions.","lang":"eng"}],"author":[{"first_name":"Jakob","full_name":"Schneider, Jakob","id":"64368429-eb97-11eb-a6c2-c980b1f44415","last_name":"Schneider"},{"full_name":"Guillerm, Undina","first_name":"Undina","id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","last_name":"Guillerm"},{"full_name":"Simoes Pereira, Caroline","first_name":"Caroline","id":"87266c4a-96d2-11ef-be2c-fe5633233ec3","last_name":"Simoes Pereira"},{"last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"file_date_updated":"2026-06-02T07:23:12Z","article_number":"e70630","oa_version":"Published Version","publication_identifier":{"issn":["0961-8368"],"eissn":["1469-896X"]},"doi":"10.1002/pro.70630","article_processing_charge":"Yes (via OA deal)","publication_status":"published","date_created":"2026-05-31T22:02:12Z","publication":"Protein Science","intvolume":"        35","citation":{"ama":"Schneider J, Guillerm U, Simoes Pereira C, Schanda P. Dynamic disorder is crucial for mitochondrial protein import. <i>Protein Science</i>. 2026;35(6). doi:<a href=\"https://doi.org/10.1002/pro.70630\">10.1002/pro.70630</a>","short":"J. Schneider, U. Guillerm, C. Simoes Pereira, P. Schanda, Protein Science 35 (2026).","chicago":"Schneider, Jakob, Undina Guillerm, Caroline Simoes Pereira, and Paul Schanda. “Dynamic Disorder Is Crucial for Mitochondrial Protein Import.” <i>Protein Science</i>. Wiley, 2026. <a href=\"https://doi.org/10.1002/pro.70630\">https://doi.org/10.1002/pro.70630</a>.","ista":"Schneider J, Guillerm U, Simoes Pereira C, Schanda P. 2026. Dynamic disorder is crucial for mitochondrial protein import. Protein Science. 35(6), e70630.","ieee":"J. Schneider, U. Guillerm, C. Simoes Pereira, and P. Schanda, “Dynamic disorder is crucial for mitochondrial protein import,” <i>Protein Science</i>, vol. 35, no. 6. Wiley, 2026.","mla":"Schneider, Jakob, et al. “Dynamic Disorder Is Crucial for Mitochondrial Protein Import.” <i>Protein Science</i>, vol. 35, no. 6, e70630, Wiley, 2026, doi:<a href=\"https://doi.org/10.1002/pro.70630\">10.1002/pro.70630</a>.","apa":"Schneider, J., Guillerm, U., Simoes Pereira, C., &#38; Schanda, P. (2026). Dynamic disorder is crucial for mitochondrial protein import. <i>Protein Science</i>. Wiley. <a href=\"https://doi.org/10.1002/pro.70630\">https://doi.org/10.1002/pro.70630</a>"},"corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","language":[{"iso":"eng"}]},{"type":"journal_article","status":"public","has_accepted_license":"1","project":[{"name":"IST Austria Open Access Fund","_id":"B67AFEDC-15C9-11EA-A837-991A96BB2854"},{"_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","grant_number":"26777"}],"issue":"1","page":"29-37","day":"16","date_updated":"2026-07-20T09:49:12Z","pmid":1,"fulldoi":"https://doi.org/10.5194/mr-7-29-2026","scopus_import":"1","ddc":["540"],"acknowledgement":"We thank Ben P. Tatman for insightful discussions. This research was supported by the Scientific Service Units (SSUs) of ISTA through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility. We thank Prof. Tobias Madl (Medical University Graz) for a sample of Omniscan. Lea M. Becker is the recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01).","quality_controlled":"1","OA_type":"gold","year":"2026","PlanS_conform":"1","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"volume":7,"month":"04","oa":1,"OA_place":"publisher","date_published":"2026-04-16T00:00:00Z","_id":"21777","publisher":"Copernicus Publications","main_file_link":[{"open_access":"1","url":"https://doi.org/10.5194/mr-7-29-2026"}],"article_type":"original","title":"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants","external_id":{"pmid":["42057802"]},"abstract":[{"lang":"eng","text":"The advantageous characteristics attributed to the 19F nucleus have made it a popular target for nuclear magnetic resonance (NMR) once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle spinning (MAS) NMR to fluorine-labelled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilised to get structural insights into proteins and measure long distances. Despite increasing popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR often suffers from slow longitudinal T1 relaxation and therefore long recycle delays. In this work, we expand paramagnetic doping, an approach commonly used to reduce proton T1 relaxation times, to 19F-labelled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F T1 and T2, and 13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labelled protein via 19F-detected MAS NMR experiments. The observed paramagnetic relaxation enhancement substantially reduces measurement times of 19F MAS NMR experiments without compromising resolution. Additionally, we report the chemical shift assignments of all four fluorotryptophan signals in the 12×39 kDa-large protein TET2 using a mutagenesis approach."}],"author":[{"full_name":"Becker, Lea Marie","first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","last_name":"Becker"},{"first_name":"Giorgia","full_name":"Toscano, Giorgia","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","last_name":"Toscano"},{"last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","full_name":"Kapitonova, Anna","first_name":"Anna"},{"full_name":"Singh, Rajkumar","first_name":"Rajkumar","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20","last_name":"Singh"},{"first_name":"Undina","full_name":"Guillerm, Undina","id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","last_name":"Guillerm"},{"last_name":"Lichtenecker","full_name":"Lichtenecker, Roman J.","first_name":"Roman J."},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"}],"oa_version":"Published Version","publication_identifier":{"eissn":["2699-0016"]},"article_processing_charge":"Yes","date_created":"2026-05-03T22:01:36Z","doi":"10.5194/mr-7-29-2026","publication_status":"published","publication":"Magnetic Resonance","citation":{"ista":"Becker LM, Toscano G, Kapitonova A, Singh R, Guillerm U, Lichtenecker RJ, Schanda P. 2026. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. Magnetic Resonance. 7(1), 29–37.","ieee":"L. M. Becker <i>et al.</i>, “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants,” <i>Magnetic Resonance</i>, vol. 7, no. 1. Copernicus Publications, pp. 29–37, 2026.","chicago":"Becker, Lea Marie, Giorgia Toscano, Anna Kapitonova, Rajkumar Singh, Undina Guillerm, Roman J. Lichtenecker, and Paul Schanda. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>. Copernicus Publications, 2026. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>.","short":"L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker, P. Schanda, Magnetic Resonance 7 (2026) 29–37.","ama":"Becker LM, Toscano G, Kapitonova A, et al. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. 2026;7(1):29-37. doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>","apa":"Becker, L. M., Toscano, G., Kapitonova, A., Singh, R., Guillerm, U., Lichtenecker, R. J., &#38; Schanda, P. (2026). Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>","mla":"Becker, Lea Marie, et al. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>, vol. 7, no. 1, Copernicus Publications, 2026, pp. 29–37, doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>."},"intvolume":"         7","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","DOAJ_listed":"1","corr_author":"1","language":[{"iso":"eng"}],"related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"22334"}]}},{"oa_version":"None","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"date_created":"2026-08-03T13:20:41Z","publication_status":"published","doi":"10.1021/jacs.6c06064","article_processing_charge":"No","abstract":[{"lang":"eng","text":"The one-bond proton-carbon coupling constant (1JCH) is an insightful probe of carbohydrate configuration. Equatorial and axial protons at the C1 position typically exhibit distinct 1JCH values, enabling NMR measurements to distinguish α- and β-configurations in carbohydrates. In principle, such measurements could provide insights into carbohydrates in the cell walls of intact microbes. However, traditionally, these measurements are performed by solution NMR with carbohydrates that were extracted, solubilized and fractionated, leaving the biological relevance of the measurements uncertain. Here, we demonstrate that 1H-detected solid-state NMR with fast magic-angle spinning allows quantitative measurements of 1JCH couplings for mobile capsular polysaccharides, directly on submilligram amounts of pathogenic cells. Our approach is demonstrated on intact cells of the pathogenic yeast Cryptococcus neoformans. High-resolution proton-detected spectra enabled the determination of coupling constants for five mobile polysaccharide units of the cryptococcal capsule, revealing their native configurations and confirming previous solution NMR-based anomeric configuration assignments."}],"author":[{"first_name":"Alons","full_name":"Lends, Alons","last_name":"Lends"},{"last_name":"Lamon","full_name":"Lamon, Gaelle","first_name":"Gaelle"},{"full_name":"Vallet, Alicia","first_name":"Alicia","last_name":"Vallet"},{"last_name":"Grélard","full_name":"Grélard, Axelle","first_name":"Axelle"},{"last_name":"Morvan","first_name":"Estelle","full_name":"Morvan, Estelle"},{"full_name":"Aimanianda, Vishukumar","first_name":"Vishukumar","last_name":"Aimanianda"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"},{"first_name":"Antoine","full_name":"Loquet, Antoine","last_name":"Loquet"}],"external_id":{"pmid":["42377973"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","language":[{"iso":"eng"}],"intvolume":"       148","citation":{"apa":"Lends, A., Lamon, G., Vallet, A., Grélard, A., Morvan, E., Aimanianda, V., … Loquet, A. (2026). On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.6c06064\">https://doi.org/10.1021/jacs.6c06064</a>","mla":"Lends, Alons, et al. “On-Cell Detection of Polysaccharide One-Bond1Jch Couplings by Proton-Detected Solid-State NMR.” <i>Journal of the American Chemical Society</i>, vol. 148, no. 27, American Chemical Society, 2026, pp. 28037–42, doi:<a href=\"https://doi.org/10.1021/jacs.6c06064\">10.1021/jacs.6c06064</a>.","ama":"Lends A, Lamon G, Vallet A, et al. On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR. <i>Journal of the American Chemical Society</i>. 2026;148(27):28037-28042. doi:<a href=\"https://doi.org/10.1021/jacs.6c06064\">10.1021/jacs.6c06064</a>","short":"A. Lends, G. Lamon, A. Vallet, A. Grélard, E. Morvan, V. Aimanianda, P. Schanda, A. Loquet, Journal of the American Chemical Society 148 (2026) 28037–28042.","ieee":"A. Lends <i>et al.</i>, “On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR,” <i>Journal of the American Chemical Society</i>, vol. 148, no. 27. American Chemical Society, pp. 28037–28042, 2026.","chicago":"Lends, Alons, Gaelle Lamon, Alicia Vallet, Axelle Grélard, Estelle Morvan, Vishukumar Aimanianda, Paul Schanda, and Antoine Loquet. “On-Cell Detection of Polysaccharide One-Bond1Jch Couplings by Proton-Detected Solid-State NMR.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2026. <a href=\"https://doi.org/10.1021/jacs.6c06064\">https://doi.org/10.1021/jacs.6c06064</a>.","ista":"Lends A, Lamon G, Vallet A, Grélard A, Morvan E, Aimanianda V, Schanda P, Loquet A. 2026. On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR. Journal of the American Chemical Society. 148(27), 28037–28042."},"publication":"Journal of the American Chemical Society","month":"06","volume":148,"date_published":"2026-06-15T00:00:00Z","das_tickbox":"0","article_type":"original","title":"On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR","_id":"22638","supplementarymaterial":"yes","publisher":"American Chemical Society","OA_type":"closed access","researchdata_availability":"no","quality_controlled":"1","acknowledgement":"We thank the ANR (ANR-16-CE11-0020-02 to A. Loquet and V.A. and ANR-21-CE17-0032 to V.A.) as well as the Swiss National Science Foundation for early postdoc mobility project P2EZP2_184258 to A. Lends. This work has benefited from the Biophysical and Structural Chemistry Platform at Institut Européen de Chimie et Biologie IECB, Centre National de la Recherche Scientifique CNRS Unité d’Appui et de Recherche UAR 3033, INSERM US001, and the CNRS (IR-RMN FR3050 and Infranalytics FR2054).","year":"2026","department":[{"_id":"PaSc"}],"issue":"27","page":"28037-28042","type":"journal_article","status":"public","scopus_import":"1","pmid":1,"fulldoi":"https://doi.org/10.1021/jacs.6c06064","day":"15","date_updated":"2026-08-04T05:52:13Z"},{"quality_controlled":"1","OA_type":"hybrid","researchdata_availability":"yes","acknowledgement":"A. Marx acknowledges the financial support of the Helmsley Fellowships Program for Sustainability and Health. A.M.B. and P.S. are supported by the Institute of Science and Technology Austria Internal Project Call grant Generative Protein NMR. S.V. was supported in part by funding from the Eric and Wendy Schmidt Center at the Broad Institute of MIT and Harvard. Open access funding provided by Institute of Science and Technology (IST Austria).","year":"2026","PlanS_conform":"1","dataavailabilitystatement":"All structures and metrics reported in this paper are openly available on Harvard Dataverse - https://doi.org/10.7910/DVN/PLYUHN. All code is openly available on GitHub (https://github.com/sai-advaith/guided_alphafold); the version used for this paper (version 0.9.1) is permanently archived on Zenodo https://doi.org/10.5281/zenodo.17307005","department":[{"_id":"PaSc"},{"_id":"AlBr"},{"_id":"GradSch"}],"type":"journal_article","status":"public","has_accepted_license":"1","scopus_import":"1","ddc":["570"],"date_updated":"2026-08-04T09:25:18Z","day":"29","fulldoi":"https://doi.org/10.1038/s41587-026-03166-5","pmid":1,"oa_version":"Published Version","publication_identifier":{"eissn":["1546-1696"],"issn":["1087-0156"]},"doi":"10.1038/s41587-026-03166-5","publication_status":"epub_ahead","article_processing_charge":"Yes (via OA deal)","date_created":"2026-07-12T22:02:19Z","external_id":{"pmid":["42374114"]},"abstract":[{"text":"AlphaFold3 predicts highly accurate protein structures from sequence but tends to collapse to a single dominant conformation, even when the underlying structure is inherently heterogeneous. Moreover, its predictions are oblivious to experimental conditions that can alter local sequence conformation. In this work, we show that AlphaFold3 can be guided to match data obtained by nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography and cryogenic electron microscopy (cryo-EM) experiments and combinations thereof. Our approach can also incorporate data that explicitly report on dynamics, such as site-resolved order parameters. We demonstrate that this methodology generates compact structural ensembles whose ensemble-averaged observables agree with experiment, with fewer distance restraint violations than traditionally resolved NMR structures and with unmodeled alternate conformations uncovered in electron density. This methodology paves the way for experimentally aware predictive models that generate structural ensembles consistent with the measurements, potentially over multiple modalities, and that can be further refined toward thermodynamically grounded ensembles by incorporating energetics.","lang":"eng"}],"author":[{"last_name":"Maddipatla","id":"e957f5e5-91c9-11f0-a95f-e090f66ecb4d","first_name":"Sai A","full_name":"Maddipatla, Sai A"},{"full_name":"Sellam, Nadav E","first_name":"Nadav E","id":"ef280fe0-91c9-11f0-a95f-8dea3f5bc513","last_name":"Sellam"},{"full_name":"Bojan, Meital I","first_name":"Meital I","id":"11d88cf5-91ca-11f0-a95f-edf9f08f47b7","last_name":"Bojan"},{"last_name":"Masalitin","full_name":"Masalitin, Vova","first_name":"Vova","id":"ff7958eb-91c9-11f0-a95f-f3bf65828cf6"},{"first_name":"Sanketh","full_name":"Vedula, Sanketh","last_name":"Vedula"},{"last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"},{"first_name":"Ailie","full_name":"Marx, Ailie","last_name":"Marx"},{"last_name":"Bronstein","id":"58f3726e-7cba-11ef-ad8b-e6e8cb3904e6","orcid":"0000-0001-9699-8730","full_name":"Bronstein, Alexander","first_name":"Alexander"}],"corr_author":"1","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","language":[{"iso":"eng"}],"related_material":{"link":[{"url":"https://ista.ac.at/en/news/toward-experiment-guided-alphafold/","relation":"press_release","description":"News on ISTA website"}]},"publication":"Nature Biotechnology","citation":{"apa":"Maddipatla, S. A., Sellam, N. E., Bojan, M. I., Masalitin, V., Vedula, S., Schanda, P., … Bronstein, A. M. (2026). Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles. <i>Nature Biotechnology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41587-026-03166-5\">https://doi.org/10.1038/s41587-026-03166-5</a>","mla":"Maddipatla, Sai A., et al. “Experiment-Guided AlphaFold3 Resolves Measurement-Consistent Protein Ensembles.” <i>Nature Biotechnology</i>, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41587-026-03166-5\">10.1038/s41587-026-03166-5</a>.","short":"S.A. Maddipatla, N.E. Sellam, M.I. Bojan, V. Masalitin, S. Vedula, P. Schanda, A. Marx, A.M. Bronstein, Nature Biotechnology (2026).","ama":"Maddipatla SA, Sellam NE, Bojan MI, et al. Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles. <i>Nature Biotechnology</i>. 2026. doi:<a href=\"https://doi.org/10.1038/s41587-026-03166-5\">10.1038/s41587-026-03166-5</a>","ieee":"S. A. Maddipatla <i>et al.</i>, “Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles,” <i>Nature Biotechnology</i>. Springer Nature, 2026.","ista":"Maddipatla SA, Sellam NE, Bojan MI, Masalitin V, Vedula S, Schanda P, Marx A, Bronstein AM. 2026. Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles. Nature Biotechnology.","chicago":"Maddipatla, Sai A, Nadav E Sellam, Meital I Bojan, Vova Masalitin, Sanketh Vedula, Paul Schanda, Ailie Marx, and Alex M. Bronstein. “Experiment-Guided AlphaFold3 Resolves Measurement-Consistent Protein Ensembles.” <i>Nature Biotechnology</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41587-026-03166-5\">https://doi.org/10.1038/s41587-026-03166-5</a>."},"month":"06","oa":1,"OA_place":"publisher","date_published":"2026-06-29T00:00:00Z","das_tickbox":"1","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"article_type":"original","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41587-026-03166-5"}],"title":"Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles","supplementarymaterial":"yes","_id":"22268","publisher":"Springer Nature"},{"_id":"22334","publisher":"Institute of Science and Technology Austria","title":"Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR","acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"NMR"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)"},"month":"07","oa":1,"das_tickbox":"1","OA_place":"publisher","date_published":"2026-07-13T00:00:00Z","citation":{"ista":"Becker LM. 2026. Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR. Institute of Science and Technology Austria.","ieee":"L. M. Becker, “Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR,” Institute of Science and Technology Austria, 2026.","chicago":"Becker, Lea Marie. “Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR.” Institute of Science and Technology Austria, 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-22334\">https://doi.org/10.15479/AT-ISTA-22334</a>.","short":"L.M. Becker, Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR, Institute of Science and Technology Austria, 2026.","ama":"Becker LM. Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR. 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22334\">10.15479/AT-ISTA-22334</a>","apa":"Becker, L. M. (2026). <i>Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-22334\">https://doi.org/10.15479/AT-ISTA-22334</a>","mla":"Becker, Lea Marie. <i>Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR</i>. Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22334\">10.15479/AT-ISTA-22334</a>."},"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","corr_author":"1","language":[{"iso":"eng"}],"related_material":{"record":[{"relation":"part_of_dissertation","status":"public","id":"12675"},{"relation":"part_of_dissertation","status":"public","id":"21777"},{"status":"public","id":"12114","relation":"part_of_dissertation"},{"relation":"part_of_dissertation","status":"public","id":"22105"}]},"abstract":[{"lang":"eng","text":"Characterizing protein dynamics at the atomic level is essential for our understanding of biological mechanisms. Whether it is to facilitate metabolite transport, catalyze reactions, transmit signals, or regulate metabolism – proteins are constantly in motion and sample multiple conformational states to fulfill their function. Nuclear magnetic resonance (NMR) spectroscopy is particularly well suited to elucidate the dynamics of biomolecules on their complex free-energy landscape. In particular, solid-state magic-angle spinning (MAS) NMR enables the study of large molecular assemblies, protein crystals, or insoluble proteins at atomic resolution without an inherent molecular size limitation. MAS NMR experiments to probe protein dynamics are extremely versatile and sensitive to motional timescales from picoseconds to seconds. Over the past decades, technological advances, developments in experimental design, and new isotope-labeling approaches have further expanded the possibilities of this technique and significantly improved the accuracy of the determined motional parameters.\r\nFunctionally important sites of proteins often contain aromatic residues. Their side-chain motions have therefore long served as valuable indicators of mechanistically relevant dynamics in NMR studies. In this thesis, site-specifically labeled aromatic residues act as sensitive reporters for MAS NMR studies of protein dynamics. The first part addresses how different environments impact side-chain motion by probing ring flips of phenylalanines and tyrosines in crystalline proteins and amyloid fibrils. It provides important insights for the analysis of dynamics obtained in non-native protein environments and emphasizes the complex factors that determine the timescale of internal dynamics. In the second part, the focus shifts towards methodological questions regarding the investigation of protein dynamics by 19F MAS NMR. The fluorine nucleus exhibits promising characteristics for NMR studies but also presents significant challenges, which is why the full methodological potential of 19F MAS NMR has not been fully realized yet. This work demonstrates that paramagnetic doping can considerably reduce the measurement time and improve the sensitivity of fluorinated samples. Finally, 19F MAS NMR is evaluated as a tool for studying protein side-chain dynamics on the example of tryptophans. The results illustrate the challenges in analyzing such experiments and lay the foundation for further development of 19F MAS NMR relaxation studies.\r\nTaken together, this thesis highlights the potential of combining specific isotope labeling, MAS NMR, and complementary methods such as crystallography and computational simulations to elucidate internal protein dynamics. The further development of such integrative approaches will be crucial to improving our understanding of complex mechanisms and protein function.\r\n"}],"author":[{"full_name":"Becker, Lea Marie","first_name":"Lea Marie","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","last_name":"Becker"}],"file_date_updated":"2026-07-16T09:17:08Z","publication_identifier":{"isbn":["978-3-99078-084-8"],"issn":["2663-337X"]},"oa_version":"Published Version","doi":"10.15479/AT-ISTA-22334","date_created":"2026-07-14T08:08:51Z","publication_status":"published","article_processing_charge":"No","date_updated":"2026-08-04T09:32:45Z","day":"13","fulldoi":"https://doi.org/10.15479/AT-ISTA-22334","ddc":["572"],"type":"dissertation","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","status":"public","has_accepted_license":"1","degree_awarded":"PhD","alternative_title":["ISTA Thesis"],"project":[{"_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches"}],"page":"205","year":"2026","file":[{"file_size":99472908,"checksum":"8b85114eff543916c0e1445cd2189555","file_id":"22346","access_level":"closed","date_created":"2026-07-16T09:17:08Z","date_updated":"2026-07-16T09:17:08Z","relation":"source_file","file_name":"2026_Becker_Lea_source_files.zip","content_type":"application/zip","creator":"lbecker"},{"success":1,"access_level":"open_access","date_created":"2026-07-16T09:17:05Z","file_id":"22347","checksum":"6c526862bc6dbd1e4c80ecb34580bc58","file_size":74647289,"date_updated":"2026-07-16T09:17:05Z","creator":"lbecker","content_type":"application/pdf","relation":"main_file","file_name":"2026_Becker_Lea_Thesis.pdf"}],"supervisor":[{"last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul"}],"doi_confirm":"1","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"acknowledgement":"During the work on this thesis, I was the recipient of a DOC Fellowship of the Austrian\r\nAcademy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01)."},{"corr_author":"1","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","language":[{"iso":"eng"}],"related_material":{"record":[{"id":"20641","status":"public","relation":"research_data"},{"relation":"research_data","id":"21145","status":"public"},{"id":"22334","status":"public","relation":"dissertation_contains"}],"link":[{"relation":"research_data","url":"https://ista.ac.at/en/news/how-proteins-breathe/","description":"News on ISTA website"}]},"publication":"Nature Chemistry","intvolume":"        18","citation":{"ista":"Becker LM, Fu H, Tatman B, Dreydoppel M, Kapitonova A, Balazs D, Weininger U, Engilberge S, Chipot C, Schanda P. 2026. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. Nature Chemistry. 18, 1221–1230.","chicago":"Becker, Lea Marie, Haohao Fu, Benjamin Tatman, Matthias Dreydoppel, Anna Kapitonova, Daniel Balazs, Ulrich Weininger, Sylvain Engilberge, Christophe Chipot, and Paul Schanda. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>.","ieee":"L. M. Becker <i>et al.</i>, “Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes,” <i>Nature Chemistry</i>, vol. 18. Springer Nature, pp. 1221–1230, 2026.","ama":"Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. 2026;18:1221-1230. doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>","short":"L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U. Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry 18 (2026) 1221–1230.","apa":"Becker, L. M., Fu, H., Tatman, B., Dreydoppel, M., Kapitonova, A., Balazs, D., … Schanda, P. (2026). Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>","mla":"Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>, vol. 18, Springer Nature, 2026, pp. 1221–30, doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>."},"publication_identifier":{"eissn":["17554349"],"issn":["17554330"]},"oa_version":"Published Version","date_created":"2026-06-21T22:03:01Z","publication_status":"published","article_processing_charge":"Yes (via OA deal)","doi":"10.1038/s41557-026-02155-0","external_id":{"pmid":["42271006"]},"abstract":[{"lang":"eng","text":"Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein–protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labelling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a crystal structure of a GB1 variant reported in this work, reproduce these elevated barriers and reveal how the crystal restrains motions."}],"author":[{"orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie","first_name":"Lea Marie","last_name":"Becker"},{"first_name":"Haohao","full_name":"Fu, Haohao","last_name":"Fu"},{"first_name":"Benjamin","full_name":"Tatman, Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman"},{"full_name":"Dreydoppel, Matthias","first_name":"Matthias","last_name":"Dreydoppel"},{"id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","full_name":"Kapitonova, Anna","first_name":"Anna","last_name":"Kapitonova"},{"orcid":"0000-0001-7597-043X","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","first_name":"Daniel","full_name":"Balazs, Daniel","last_name":"Balazs"},{"first_name":"Ulrich","full_name":"Weininger, Ulrich","last_name":"Weininger"},{"last_name":"Engilberge","first_name":"Sylvain","full_name":"Engilberge, Sylvain"},{"first_name":"Christophe","full_name":"Chipot, Christophe","last_name":"Chipot"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"file_date_updated":"2026-07-28T06:58:35Z","article_type":"original","title":"Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes","_id":"22105","supplementarymaterial":"yes","publisher":"Springer Nature","volume":18,"month":"07","oa":1,"date_published":"2026-07-01T00:00:00Z","das_tickbox":"1","OA_place":"publisher","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"year":"2026","PlanS_conform":"1","file":[{"success":1,"checksum":"1069fb27949fd2cb641b043b3a96a580","access_level":"open_access","file_id":"22595","date_created":"2026-07-28T06:58:35Z","file_size":2618184,"date_updated":"2026-07-28T06:58:35Z","creator":"dernst","file_name":"2026_NatureChemistry_Becker.pdf","relation":"main_file","content_type":"application/pdf"}],"dataavailabilitystatement":"The cryo and room-temperature crystal structures of GB1QDD are deposited at the PDB under the access codes 9I2I and 9T8Z, respectively. The solid-state NMR backbone assignment of GB1QDD is deposited at the BMRB under the access code 53330. NMR spectra, analysis scripts and raw data are publicly available at the ISTA research explorer (https://doi.org/10.15479/AT-ISTA-20641)120. Files to reproduce the enhanced-sampling MD simulations are publicly available at the ISTA research explorer (https://doi.org/10.15479/AT-ISTA-21145)121.","department":[{"_id":"PaSc"},{"_id":"LifeSc"}],"quality_controlled":"1","researchdata_availability":"yes","OA_type":"hybrid","acknowledgement":"We thank N. R. Skrynnikov and O. O. Lebedenko (St. Petersburg) for insightful discussions and for performing exploratory MD simulations. We are grateful to T. Schubeis (Lyon) for advice on GB1 crystallization and R. Schmid for initial crystallization trials. We thank C. Mueller-Dieckmann for assistance with room-temperature X-ray crystallography data collection on beamline ID30B at the ESRF, which is acknowledged for providing beamtime through its In-House Research programme. We thank S. Falkner for assistance with constructing the structural model of the IgG:GB1 complex. We thank J. Lewandowski for providing feedback on the paper and granting access to backbone relaxation data of IgG:GB1T2Q and GB1T2Q microcrystals. This research was supported by the Scientific Service Units (SSU) of the Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank P. Rovó and M. V. Falcón for excellent support of the NMR facility. L.M.B. is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant number PR10660EAW01). C.C. acknowledges the European Research Council (grant project 101097272 ‘MilliInMicro’) and the Métropole du Grand Nancy (grant project ‘ARC’). BM07-FIP2 is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under grant agreement ANR-21-ESRE-0011.Open access funding provided by Institute of Science and Technology (IST Austria).","scopus_import":"1","ddc":["540"],"day":"01","date_updated":"2026-08-04T09:32:45Z","pmid":1,"fulldoi":"https://doi.org/10.1038/s41557-026-02155-0","project":[{"grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0"}],"page":"1221-1230","type":"journal_article","status":"public","has_accepted_license":"1"},{"acknowledgement":"We thank Nikolai R. Skrynnikov and Olga O. Lebedenko (St. Petersburg) for insightful discussions and for performing exploratory MD simulations. We are grateful to Tobias Schubeis (Lyon) for advice with GB1 crystallization, and Rebecca Schmid for initial crystallization trials.\r\nWe thank Sebastian Falkner for assistance with constructing the structural model of the IgG:GB1 complex.\r\nThis research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra Rovó and Margarita Valhondo Falcón for excellent support of the NMR facility.\r\nLea M. Becker is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01). Christophe Chipot acknowledges the European Research Council (grant project 101097272 ``MilliInMicro'') and the Métropole du Grand Nancy (grant project ``ARC''). BM07-FIP2 is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under grant agreement ANR-21-ESRE-0011.","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"year":"2026","file":[{"checksum":"02a419cce8cea450bc952f35488d2df5","file_id":"21146","access_level":"open_access","date_created":"2026-02-05T13:52:37Z","file_size":4263,"creator":"lbecker","relation":"table_of_contents","file_name":"README.txt","content_type":"text/plain","date_updated":"2026-02-05T13:52:37Z"},{"creator":"lbecker","relation":"main_file","file_name":"Research_Data.zip","content_type":"application/zip","date_updated":"2026-02-05T13:52:41Z","checksum":"b0b82b1aa73985b0b308a3fa52d21aea","date_created":"2026-02-05T13:52:41Z","access_level":"open_access","file_id":"21147","file_size":50647107,"success":1}],"status":"public","has_accepted_license":"1","type":"research_data","project":[{"_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches"}],"date_updated":"2026-08-04T09:32:45Z","day":"09","contributor":[{"contributor_type":"researcher","last_name":"Fu","first_name":"Haohao"},{"first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Dreydoppel","first_name":"Matthias"},{"first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","last_name":"Kapitonova","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Balazs","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","orcid":"0000-0001-7597-043X","first_name":"Daniel"},{"contributor_type":"researcher","last_name":"Weininger","first_name":"Ulrich"},{"contributor_type":"researcher","last_name":"Engilberge","first_name":"Sylvain"}],"fulldoi":"https://doi.org/10.15479/AT-ISTA-21145","ddc":["572"],"file_date_updated":"2026-02-05T13:52:41Z","abstract":[{"lang":"eng","text":"Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. "}],"author":[{"last_name":"Becker","full_name":"Becker, Lea Marie","first_name":"Lea Marie","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79"},{"last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Chipot","full_name":"Chipot, Christophe","first_name":"Christophe"}],"article_processing_charge":"No","doi":"10.15479/AT-ISTA-21145","date_created":"2026-02-05T13:54:39Z","oa_version":"Published Version","citation":{"ama":"Becker LM, Schanda P, Chipot C. Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21145\">10.15479/AT-ISTA-21145</a>","short":"L.M. Becker, P. Schanda, C. Chipot, (2026).","ista":"Becker LM, Schanda P, Chipot C. 2026. Additional Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-21145\">10.15479/AT-ISTA-21145</a>.","ieee":"L. M. Becker, P. Schanda, and C. Chipot, “Additional Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2026.","chicago":"Becker, Lea Marie, Paul Schanda, and Christophe Chipot. “Additional Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-21145\">https://doi.org/10.15479/AT-ISTA-21145</a>.","apa":"Becker, L. M., Schanda, P., &#38; Chipot, C. (2026). Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-21145\">https://doi.org/10.15479/AT-ISTA-21145</a>","mla":"Becker, Lea Marie, et al. <i>Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.”</i> Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21145\">10.15479/AT-ISTA-21145</a>."},"related_material":{"record":[{"id":"20641","status":"public","relation":"earlier_version"},{"relation":"used_in_publication","id":"22105","status":"public"}]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","corr_author":"1","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","image":"/images/cc_by_nc.png","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"oa":1,"date_published":"2026-02-09T00:00:00Z","month":"02","publisher":"Institute of Science and Technology Austria","_id":"21145","title":"Additional Data for \"Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes\""},{"file_date_updated":"2026-08-18T06:33:14Z","external_id":{"arxiv":["2505.23354"]},"abstract":[{"lang":"eng","text":"The local structure of a protein strongly impacts its function and interactions\r\nwith other molecules. Representing local biomolecular environments remains a\r\nkey challenge while applying machine learning approaches over protein structures. The structural and chemical variability of these environments makes them\r\nchallenging to model, and performing representation learning on these objects\r\nremains largely under-explored. In this work, we propose representations for\r\nlocal protein environments that leverage intermediate features from machine learning force fields (MLFFs). We extensively benchmark state-of-the-art MLFFs,\r\ncomparing their performance across latent spaces and downstream tasks, and\r\nshow that their embeddings capture local structural (e.g., secondary motifs) and\r\nchemical features (e.g., amino acid identity and protonation state), organizing\r\nprotein environments into a structured manifold. We show that these representations enable zero-shot generalization and transfer across diverse downstream\r\ntasks. As a case study, we build a physics-informed, uncertainty-aware chemical shift predictor that achieves state-of-the-art accuracy in biomolecular NMR\r\nspectroscopy. Our results establish MLFFs as general-purpose, reusable representation learners for protein modeling, opening new directions in representation learning for structured physical systems. Code and data are available at\r\nhttps://github.com/mb012/MLFF_representation.\r\n"}],"author":[{"id":"11d88cf5-91ca-11f0-a95f-edf9f08f47b7","full_name":"Bojan, Meital I","first_name":"Meital I","last_name":"Bojan"},{"last_name":"Vedula","first_name":"Sanketh","full_name":"Vedula, Sanketh"},{"last_name":"Maddipatla","first_name":"Sai A","full_name":"Maddipatla, Sai A","id":"e957f5e5-91c9-11f0-a95f-e090f66ecb4d"},{"id":"ef280fe0-91c9-11f0-a95f-8dea3f5bc513","full_name":"Sellam, Nadav E","first_name":"Nadav E","last_name":"Sellam"},{"last_name":"Rzayev","first_name":"Anar","full_name":"Rzayev, Anar","id":"2cd60677-9acd-11f1-ae1a-a85ae1c4dd35"},{"last_name":"Napoli","first_name":"Federico","full_name":"Napoli, Federico","orcid":"0000-0002-9043-136X","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b"},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul"},{"last_name":"Bronstein","first_name":"Alexander","full_name":"Bronstein, Alexander","orcid":"0000-0001-9699-8730","id":"58f3726e-7cba-11ef-ad8b-e6e8cb3904e6"}],"date_created":"2026-08-17T12:03:24Z","publication_status":"published","article_processing_charge":"No","oa_version":"Published Version","publication":"14th International Conference on Learning Representations","intvolume":"      2026","citation":{"chicago":"Bojan, Meital I, Sanketh Vedula, Sai A Maddipatla, Nadav E Sellam, Anar Rzayev, Federico Napoli, Paul Schanda, and Alex M. Bronstein. “Representing Local Protein Environments with Machine Learning Force Fields.” In <i>14th International Conference on Learning Representations</i>, 2026:100760–99, 2026.","ieee":"M. I. Bojan <i>et al.</i>, “Representing local protein environments with machine learning force fields,” in <i>14th International Conference on Learning Representations</i>, Rio de Janeiro, Brazil, 2026, vol. 2026, pp. 100760–100799.","ista":"Bojan MI, Vedula S, Maddipatla SA, Sellam NE, Rzayev A, Napoli F, Schanda P, Bronstein AM. 2026. Representing local protein environments with machine learning force fields. 14th International Conference on Learning Representations. ICLR: International Conference on Learning Representations vol. 2026, 100760–100799.","ama":"Bojan MI, Vedula S, Maddipatla SA, et al. Representing local protein environments with machine learning force fields. In: <i>14th International Conference on Learning Representations</i>. Vol 2026. ; 2026:100760-100799.","short":"M.I. Bojan, S. Vedula, S.A. Maddipatla, N.E. Sellam, A. Rzayev, F. Napoli, P. Schanda, A.M. Bronstein, in:, 14th International Conference on Learning Representations, 2026, pp. 100760–100799.","mla":"Bojan, Meital I., et al. “Representing Local Protein Environments with Machine Learning Force Fields.” <i>14th International Conference on Learning Representations</i>, vol. 2026, 2026, pp. 100760–99.","apa":"Bojan, M. I., Vedula, S., Maddipatla, S. A., Sellam, N. E., Rzayev, A., Napoli, F., … Bronstein, A. M. (2026). Representing local protein environments with machine learning force fields. In <i>14th International Conference on Learning Representations</i> (Vol. 2026, pp. 100760–100799). Rio de Janeiro, Brazil."},"language":[{"iso":"eng"}],"related_material":{"link":[{"url":"https://github.com/mb012/MLFF_representation","relation":"software"}]},"corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"acknowledged_ssus":[{"_id":"ScienComp"}],"oa":1,"OA_place":"publisher","date_published":"2026-05-01T00:00:00Z","das_tickbox":"1","volume":2026,"month":"05","supplementarymaterial":"yes","_id":"22722","title":"Representing local protein environments with machine learning force fields","acknowledgement":"This work was supported by the Institute of Science and Technology Austria (ISTA) through the IPC\r\ngrant “Generative Protein NMR” and by the Israeli Science Foundation (ISF) under grant number\r\n1834/24. This research used resources of the Institute of Science and Technology Austria’s scientific\r\ncomputing cluster. S.V. was supported in part by funding from the Eric and Wendy Schmidt Center at\r\nthe Broad Institute of MIT and Harvard.","quality_controlled":"1","OA_type":"gold","conference":{"end_date":"2026-04-27","location":"Rio de Janeiro, Brazil","start_date":"2026-04-23","name":"ICLR: International Conference on Learning Representations"},"researchdata_availability":"yes","arxiv":1,"dataavailabilitystatement":"The code, trained models, and data-processing scripts are publicly available at https://github.\r\ncom/mb012/MLFF_representation. In addition, complete details of the models and optimization parameters are provided in Appendix G.3. The hardware resources used to produce the\r\nresults are specified in Appendix I.4. The loss functions, evaluation metrics, and details regarding\r\nablation studies are specified in Appendix G. These details ensure that all results reported in the paper\r\ncan be independently verified.","department":[{"_id":"GradSch"},{"_id":"PaSc"},{"_id":"AlBr"}],"year":"2026","file":[{"success":1,"file_size":8534339,"access_level":"open_access","date_created":"2026-08-18T06:33:14Z","file_id":"22723","checksum":"9f43f5469443388ec55388d95c4cf243","date_updated":"2026-08-18T06:33:14Z","content_type":"application/pdf","file_name":"2026_ICLR_Bojan.pdf","relation":"main_file","creator":"dernst"}],"status":"public","has_accepted_license":"1","type":"conference","page":"100760-100799","day":"01","date_updated":"2026-08-18T06:36:55Z","ddc":["000","570"]},{"publisher":"Institute of Science and Technology Austria","_id":"22687","title":"Data and scripts for: \"Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme\"","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","image":"/images/cc_by_nc.png","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"OA_place":"repository","date_published":"2026-08-20T00:00:00Z","oa":1,"month":"08","citation":{"apa":"Schanda, P., &#38; Napoli, F. (2026). Data and scripts for: “Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-22687\">https://doi.org/10.15479/AT-ISTA-22687</a>","mla":"Schanda, Paul, and Federico Napoli. <i>Data and Scripts for: “Integrated Solid/Solution NMR Assignment Allows Mapping Dynamics and Ligand Binding in a 134 KDa Enzyme.”</i> Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22687\">10.15479/AT-ISTA-22687</a>.","short":"P. Schanda, F. Napoli, (2026).","ama":"Schanda P, Napoli F. Data and scripts for: “Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.” 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22687\">10.15479/AT-ISTA-22687</a>","ista":"Schanda P, Napoli F. 2026. Data and scripts for: ‘Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-22687\">10.15479/AT-ISTA-22687</a>.","ieee":"P. Schanda and F. Napoli, “Data and scripts for: ‘Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.’” Institute of Science and Technology Austria, 2026.","chicago":"Schanda, Paul, and Federico Napoli. “Data and Scripts for: ‘Integrated Solid/Solution NMR Assignment Allows Mapping Dynamics and Ligand Binding in a 134 KDa Enzyme.’” Institute of Science and Technology Austria, 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-22687\">https://doi.org/10.15479/AT-ISTA-22687</a>."},"user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","corr_author":"1","file_date_updated":"2026-08-20T07:35:05Z","author":[{"last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul"},{"first_name":"Federico","full_name":"Napoli, Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","orcid":"0000-0002-9043-136X","last_name":"Napoli"}],"abstract":[{"lang":"eng","text":"Understanding enzyme function requires characterizing not only static structure but also dynamics and ligand interactions. NMR spectroscopy provides this insight at atomic resolution, yet for large proteins the difficulty of resonance assignment has largely confined such studies to systems below ∼50 kDa, or to observing only methyl groups. Here we present an integrated magic-angle spinning (MAS) and solution NMR study of the 134 kDa tetrameric malate dehydrogenase from Ignicoccus islandicus (IiMDH), an enzyme of particular interest as an evolutionary intermediate between allosteric lactate\r\ndehydrogenases and non-allosteric malate dehydrogenases. By combining high-dimensional (up to 4D) MAS NMR experiments on sedimented protein with solution NMR, we achieved 92% backbone heavy- atom assignment and 91% assignment of all Ile-δ1, Leu-δ1/-δ2, Val-γ1/-γ2, Met-ε and Thr-γ methyl groups. Building on these assignments, we use various probes of backbone and sidechain dynamics: elevated MAS NMR 15N rotating-frame relaxation (R1ρ) points to microsecond motions in functionally critical regions, including the catalytic loop and the mobile surface loop. Complementary methyl-axis order parameters from solution NMR identified additional flexible sites in the hydrophobic core. Chemical shift perturbation experiments upon addition of the substrate analogue oxamate, monitored via backbone 1H-15N TROSY, revealed both active-site contacts and responses in helices α2F and α3G, regions implicated in allosteric signal transmission. The integrated approach demonstrated here exploits the distinct strengths of MAS and solution NMR, and provides a comprehensive view of structure, dynamics, and substrate interactions in a large oligomeric enzyme that would not be accessible by either technique alone."}],"article_processing_charge":"No","doi":"10.15479/AT-ISTA-22687","date_created":"2026-08-12T16:12:19Z","oa_version":"None","fulldoi":"https://doi.org/10.15479/AT-ISTA-22687","contributor":[{"id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","orcid":"0000-0002-9043-136X","first_name":"Federico","contributor_type":"researcher","last_name":"Napoli"},{"first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","contributor_type":"project_leader"},{"last_name":"Singh","contributor_type":"project_member","first_name":"Rajkumar","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20"},{"contributor_type":"project_member","last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna"},{"first_name":"Virgil","contributor_type":"project_member","last_name":"Aitenbichler"},{"last_name":"Toscano","contributor_type":"project_member","first_name":"Giorgia","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4"},{"contributor_type":"data_collector","last_name":"Perrone","first_name":"Barbara"}],"date_updated":"2026-08-20T07:40:15Z","day":"20","has_accepted_license":"1","status":"public","type":"research_data","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}],"doi_confirm":"1","department":[{"_id":"PaSc"}],"file":[{"date_updated":"2026-08-18T07:13:26Z","relation":"main_file","file_name":"Pulse_parameters.xlsx","content_type":"application/vnd.openxmlformats-officedocument.spreadsheetml.sheet","creator":"fnapoli","success":1,"file_size":59096,"checksum":"dd23db23f7e75bafad6c67381163c1e2","access_level":"open_access","file_id":"22725","date_created":"2026-08-18T07:13:26Z"},{"success":1,"file_size":3591173,"checksum":"a7ad194d8d7f780725bc2c60c63d686d","file_id":"22726","access_level":"open_access","date_created":"2026-08-18T07:16:00Z","date_updated":"2026-08-18T07:16:00Z","file_name":"Scripts_submission.zip","relation":"main_file","content_type":"application/zip","creator":"fnapoli"},{"success":1,"file_size":28750919,"date_created":"2026-08-18T07:15:59Z","file_id":"22727","access_level":"open_access","checksum":"dc099c298844973512ab224464964a1a","date_updated":"2026-08-18T07:15:59Z","content_type":"application/zip","file_name":"FLYA_runs.zip","relation":"main_file","creator":"fnapoli"},{"relation":"main_file","file_name":"spectra_Bruker.zip","content_type":"application/zip","creator":"fnapoli","date_updated":"2026-08-18T07:33:47Z","file_size":3824856998,"checksum":"04bcce8eb20c90089cbd2fb5e0c50a7f","file_id":"22728","date_created":"2026-08-18T07:33:47Z","access_level":"open_access","success":1},{"file_id":"22729","date_created":"2026-08-18T08:03:33Z","access_level":"open_access","checksum":"91c1161ca98632ed643d2b564395da5b","file_size":17880653,"success":1,"creator":"fnapoli","content_type":"application/zip","relation":"main_file","file_name":"Titration_data.zip","date_updated":"2026-08-18T08:03:33Z"},{"checksum":"ca2cf03b82656ae2858931d4391a3158","file_id":"22743","date_created":"2026-08-20T07:35:05Z","access_level":"open_access","file_size":868,"success":1,"creator":"arashid","relation":"main_file","file_name":"README.txt","content_type":"text/plain","date_updated":"2026-08-20T07:35:05Z"}],"year":"2026","acknowledgement":"This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra Rovó, Megha Mohan and Margarita Valhondo Falcón for excellent support of the NMR facility."},{"ddc":["570"],"scopus_import":"1","fulldoi":"https://doi.org/10.1093/bioadv/vbag182","pmid":1,"date_updated":"2026-10-01T08:59:32Z","day":"06","issue":"1","has_accepted_license":"1","status":"public","type":"journal_article","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"dataavailabilitystatement":"The data underlying this article, including the abstract books for\r\nthe first and second editions of the SEH2Bioinfo symposia, are\r\navailable in Zenodo at https://doi.org/10.5281/zenodo.6603621\r\nand https://doi.org/10.5281/zenodo.1,54,46,570, respectively.","file":[{"file_size":1359968,"checksum":"8885b0531a655103c46899b2f935b0db","access_level":"open_access","date_created":"2026-10-01T08:55:00Z","file_id":"23016","success":1,"file_name":"2026_BioinformaticsAdvances_Franzotti.pdf","relation":"main_file","content_type":"application/pdf","creator":"dernst","date_updated":"2026-10-01T08:55:00Z"}],"year":"2026","OA_type":"gold","researchdata_availability":"yes","quality_controlled":"1","acknowledgement":"We acknowledge the sponsors who made the SEH2Bioinfo possible, the organizers from the various Spanish-speaking RSGs, and\r\nthe collaborators who contributed to dissemination, logistics,\r\nand other essential tasks for its execution. G.J.O.-O. thanks the\r\nFONDECYT Postdoctoral Project No. 3250793 for financial support. G.J.O.-O. also expresses gratitude to Valentina Luza: “May\r\nher passion for science communication keep inspiring new generations, myself included, to infinity and beyond!” R.G.P.\r\nthanks the Argentinian public university education system as an\r\nelement of social ascendance and democratization of professional opportunities.","title":"Bioinformatics in Español: Expanding open, diverse, and collaborative science through SEH2Bioinfo","article_type":"original","publisher":"Oxford University Press","_id":"22957","supplementarymaterial":"no","OA_place":"publisher","date_published":"2026-08-06T00:00:00Z","das_tickbox":"1","oa":1,"month":"08","volume":6,"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"related_material":{"link":[{"url":"https://doi.org/10.1093/bioadv/vbag271","relation":"erratum"}]},"language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","DOAJ_listed":"1","intvolume":"         6","citation":{"chicago":"Padilla Franzotti, Carla L, Gabriel J Olguín-Orellana, Nicolas Palopoli, Sebastián Urquiza-Zurich, Adrian Garcia-Moreno, Sara Monzón, Mónica Cabrera-Pasadas, et al. “Bioinformatics in Español: Expanding Open, Diverse, and Collaborative Science through SEH2Bioinfo.” <i>Bioinformatics Advances</i>. Oxford University Press, 2026. <a href=\"https://doi.org/10.1093/bioadv/vbag182\">https://doi.org/10.1093/bioadv/vbag182</a>.","ieee":"C. L. Padilla Franzotti <i>et al.</i>, “Bioinformatics in Español: Expanding open, diverse, and collaborative science through SEH2Bioinfo,” <i>Bioinformatics Advances</i>, vol. 6, no. 1. Oxford University Press, 2026.","ista":"Padilla Franzotti CL, Olguín-Orellana GJ, Palopoli N, Urquiza-Zurich S, Garcia-Moreno A, Monzón S, Cabrera-Pasadas M, Soler Sáez I, Perpiñá-Clérigues C, Puche Quiñonez RJ, Vélez Segura J, Lovaco-Flores JA, Osorio Mogollón CM, Esquinas-Román EM, Miserendino MC, Eranti P, Castillo-Orozco A, Cuesta-Astroz Y, Parra RG. 2026. Bioinformatics in Español: Expanding open, diverse, and collaborative science through SEH2Bioinfo. Bioinformatics Advances. 6(1), vbag182.","ama":"Padilla Franzotti CL, Olguín-Orellana GJ, Palopoli N, et al. Bioinformatics in Español: Expanding open, diverse, and collaborative science through SEH2Bioinfo. <i>Bioinformatics Advances</i>. 2026;6(1). doi:<a href=\"https://doi.org/10.1093/bioadv/vbag182\">10.1093/bioadv/vbag182</a>","short":"C.L. Padilla Franzotti, G.J. Olguín-Orellana, N. Palopoli, S. Urquiza-Zurich, A. Garcia-Moreno, S. Monzón, M. Cabrera-Pasadas, I. Soler Sáez, C. Perpiñá-Clérigues, R.J. Puche Quiñonez, J. Vélez Segura, J.A. Lovaco-Flores, C.M. Osorio Mogollón, E.M. Esquinas-Román, M.C. Miserendino, P. Eranti, A. Castillo-Orozco, Y. Cuesta-Astroz, R.G. Parra, Bioinformatics Advances 6 (2026).","mla":"Padilla Franzotti, Carla L., et al. “Bioinformatics in Español: Expanding Open, Diverse, and Collaborative Science through SEH2Bioinfo.” <i>Bioinformatics Advances</i>, vol. 6, no. 1, vbag182, Oxford University Press, 2026, doi:<a href=\"https://doi.org/10.1093/bioadv/vbag182\">10.1093/bioadv/vbag182</a>.","apa":"Padilla Franzotti, C. L., Olguín-Orellana, G. J., Palopoli, N., Urquiza-Zurich, S., Garcia-Moreno, A., Monzón, S., … Parra, R. G. (2026). Bioinformatics in Español: Expanding open, diverse, and collaborative science through SEH2Bioinfo. <i>Bioinformatics Advances</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/bioadv/vbag182\">https://doi.org/10.1093/bioadv/vbag182</a>"},"publication":"Bioinformatics Advances","article_processing_charge":"Yes","doi":"10.1093/bioadv/vbag182","publication_status":"published","date_created":"2026-09-17T11:06:17Z","oa_version":"Published Version","publication_identifier":{"eissn":["2635-0041"]},"article_number":"vbag182","file_date_updated":"2026-10-01T08:55:00Z","abstract":[{"text":"Linguistic inequality remains a silent barrier in contemporary science, particularly in rapidly evolving and interdisciplinary fields such as bioinformatics. This article examines how the Spanish-speaking community has responded to this gap through the creation of the Simposio de Estudiantes Hispanohablantes de Bioinformática y Biología Computacional (SEH2Bioinfo), a collective initiative that transforms language into a tool for inclusion and collaboration. Drawing on a historical review of the use of Spanish in scientific communication and an analysis of the two editions of SEH2Bioinfo (2022 and 2025), complemented by surveys of more than 1500 participants, we explore the effects of language on confidence, participation, and academic visibility. The findings show that Spanish can serve as a space for training and mentorship without compromising rigor, while simultaneously strengthening international networks and promoting open science. The growth of SEH2Bioinfo, its collaborative approach, and its intercontinental reach establish the symposium as a model for linguistic equity in scientific practice. Its experience demonstrates that expanding linguistic diversity in bioinformatics is not only possible but essential to building a global scientific community that is fairer, more connected, and representative.","lang":"eng"}],"author":[{"last_name":"Padilla Franzotti","first_name":"Carla L","full_name":"Padilla Franzotti, Carla L"},{"last_name":"Olguín-Orellana","full_name":"Olguín-Orellana, Gabriel J","first_name":"Gabriel J"},{"first_name":"Nicolas","full_name":"Palopoli, Nicolas","last_name":"Palopoli"},{"first_name":"Sebastián","full_name":"Urquiza-Zurich, Sebastián","last_name":"Urquiza-Zurich"},{"last_name":"Garcia-Moreno","first_name":"Adrian","full_name":"Garcia-Moreno, Adrian"},{"first_name":"Sara","full_name":"Monzón, Sara","last_name":"Monzón"},{"last_name":"Cabrera-Pasadas","full_name":"Cabrera-Pasadas, Mónica","first_name":"Mónica"},{"first_name":"Irene","full_name":"Soler Sáez, Irene","last_name":"Soler Sáez"},{"full_name":"Perpiñá-Clérigues, Carla","first_name":"Carla","last_name":"Perpiñá-Clérigues"},{"full_name":"Puche Quiñonez, Rafael J","first_name":"Rafael J","last_name":"Puche Quiñonez"},{"first_name":"Jennifer","full_name":"Vélez Segura, Jennifer","last_name":"Vélez Segura"},{"last_name":"Lovaco-Flores","first_name":"Jose Abel","full_name":"Lovaco-Flores, Jose Abel"},{"last_name":"Osorio Mogollón","first_name":"Cleidy M","full_name":"Osorio Mogollón, Cleidy M"},{"last_name":"Esquinas-Román","full_name":"Esquinas-Román, Eva M","first_name":"Eva M"},{"last_name":"Miserendino","first_name":"Maria C","full_name":"Miserendino, Maria C","id":"273e0cbd-72f0-11ef-b75a-f9f932e292fa"},{"first_name":"Pradeep","full_name":"Eranti, Pradeep","last_name":"Eranti"},{"last_name":"Castillo-Orozco","first_name":"Ana","full_name":"Castillo-Orozco, Ana"},{"first_name":"Yesid","full_name":"Cuesta-Astroz, Yesid","last_name":"Cuesta-Astroz"},{"first_name":"R Gonzalo","full_name":"Parra, R Gonzalo","last_name":"Parra"}],"external_id":{"pmid":["42577783"]}},{"corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","language":[{"iso":"eng"}],"citation":{"apa":"Tatman, B., &#38; Schanda, P. (2026). Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">https://doi.org/10.1016/j.pnmrs.2026.101615</a>","mla":"Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics by Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157, 101615, Elsevier, 2026, doi:<a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">10.1016/j.pnmrs.2026.101615</a>.","chicago":"Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics by Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier, 2026. <a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">https://doi.org/10.1016/j.pnmrs.2026.101615</a>.","ieee":"B. Tatman and P. Schanda, “Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches,” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157. Elsevier, 2026.","ista":"Tatman B, Schanda P. 2026. Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. Progress in Nuclear Magnetic Resonance Spectroscopy. 156–157, 101615.","short":"B. Tatman, P. Schanda, Progress in Nuclear Magnetic Resonance Spectroscopy 156–157 (2026).","ama":"Tatman B, Schanda P. Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. 2026;156-157. doi:<a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">10.1016/j.pnmrs.2026.101615</a>"},"publication":"Progress in Nuclear Magnetic Resonance Spectroscopy","oa_version":"Published Version","publication_identifier":{"eissn":["1873-3301"],"issn":["0079-6565"]},"article_processing_charge":"Yes (via OA deal)","date_created":"2026-09-22T05:44:22Z","publication_status":"epub_ahead","doi":"10.1016/j.pnmrs.2026.101615","abstract":[{"text":"Far from being static structures, it is now well accepted that proteins are highly dynamic entities even in the solid state. Here, we review recent progress in application of magic-angle spinning (MAS) NMR for studying the site-specific dynamics of proteins, as assessed using spin-relaxation and measurement of anisotropic spin interactions. We focus on the types of experimental data that are available, and how best to access the information which is provided by these experimental measurements; in particular, we provide a retrospective on the field in light of recent advances in analytical methodologies, which have led to a slow paradigm shift in how we interpret relaxation rate constant measurements made in the solid state.","lang":"eng"}],"author":[{"last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin","first_name":"Benjamin"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"}],"article_number":"101615","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.pnmrs.2026.101615"}],"article_type":"original","title":"Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches","_id":"22974","supplementarymaterial":"yes","publisher":"Elsevier","volume":"156-157","month":"09","das_tickbox":"1","OA_place":"publisher","date_published":"2026-09-01T00:00:00Z","oa":1,"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"year":"2026","department":[{"_id":"PaSc"}],"dataavailabilitystatement":"No data was used for the research described in the article.","OA_type":"hybrid","researchdata_availability":"no","keyword":["Solid-state NMR","Protein dynamics","Magic-angle spinning"],"quality_controlled":"1","acknowledgement":"We thank the Austrian Science Fund (FWF, project number 10.55776/I5812) for support. We are grateful to Petra Rovó (ISTA) for many insightful discussions.","scopus_import":"1","ddc":["540"],"fulldoi":"https://doi.org/10.1016/j.pnmrs.2026.101615","day":"01","date_updated":"2026-10-06T13:00:47Z","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"}],"type":"journal_article","has_accepted_license":"1","status":"public"},{"volume":267,"month":"07","oa":1,"date_published":"2025-07-30T00:00:00Z","OA_place":"publisher","acknowledged_ssus":[{"_id":"ScienComp"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"title":"Inverse problems with experiment-guided AlphaFold","_id":"21327","publisher":"ML Research Press","oa_version":"Published Version","publication_identifier":{"eissn":["2640-3498"]},"date_created":"2026-02-18T12:11:17Z","article_processing_charge":"No","publication_status":"published","external_id":{"arxiv":["2502.09372"]},"author":[{"id":"e957f5e5-91c9-11f0-a95f-e090f66ecb4d","first_name":"Sai A","full_name":"Maddipatla, Sai A","last_name":"Maddipatla"},{"last_name":"Sellam","first_name":"Nadav E","full_name":"Sellam, Nadav E","id":"ef280fe0-91c9-11f0-a95f-8dea3f5bc513"},{"id":"11d88cf5-91ca-11f0-a95f-edf9f08f47b7","full_name":"Bojan, Meital I","first_name":"Meital I","last_name":"Bojan"},{"last_name":"Vedula","full_name":"Vedula, Sanketh","first_name":"Sanketh","id":"94f2fe44-70fa-11f0-b76b-92922c09452b"},{"last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul"},{"last_name":"Marx","full_name":"Marx, Ailie","first_name":"Ailie"},{"last_name":"Bronstein","full_name":"Bronstein, Alexander","first_name":"Alexander","id":"58f3726e-7cba-11ef-ad8b-e6e8cb3904e6","orcid":"0000-0001-9699-8730"}],"abstract":[{"text":"Proteins exist as a dynamic ensemble of multiple conformations, and these motions are often crucial for their functions. However, current structure prediction methods predominantly yield a single conformation, overlooking the conformational heterogeneity revealed by diverse experimental modalities. Here, we present a framework for building experiment-grounded protein structure generative models that infer conformational ensembles consistent with measured experimental data. The key idea is to treat stateof-the-art protein structure predictors (e.g., AlphaFold3) as sequence-conditioned structural priors, and cast ensemble modeling as posterior inference of protein structures given experimental measurements. Through extensive real-data experiments, we demonstrate the generality of our method to incorporate a variety of experimental measurements. In particular, our framework uncovers previously unmodeled conformational heterogeneity from crystallographic densities, and generates high-accuracy NMR ensembles orders of magnitude faster than the status quo. Notably, we demonstrate that our ensembles outperform AlphaFold3 (Abramson et al., 2024) and sometimes better fit experimental data than publicly deposited structures to the Protein Data Bank (PDB, Burley et al. (2017)). We believe that this approach will unlock building predictive models that fully embrace experimentally observed conformational diversity.","lang":"eng"}],"file_date_updated":"2026-02-19T08:56:10Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","corr_author":"1","language":[{"iso":"eng"}],"publication":"Proceedings of the 42nd International Conference on Machine Learning","intvolume":"       267","citation":{"ista":"Maddipatla SA, Sellam NE, Bojan MI, Vedula S, Schanda P, Marx A, Bronstein AM. 2025. Inverse problems with experiment-guided AlphaFold. Proceedings of the 42nd International Conference on Machine Learning. ICML: International Conference on Machine Learning, PMLR, vol. 267, 42366–42393.","chicago":"Maddipatla, Sai A, Nadav E Sellam, Meital I Bojan, Sanketh Vedula, Paul Schanda, Ailie Marx, and Alex M. Bronstein. “Inverse Problems with Experiment-Guided AlphaFold.” In <i>Proceedings of the 42nd International Conference on Machine Learning</i>, 267:42366–93. ML Research Press, 2025.","ieee":"S. A. Maddipatla <i>et al.</i>, “Inverse problems with experiment-guided AlphaFold,” in <i>Proceedings of the 42nd International Conference on Machine Learning</i>, Vancouver, Canada, 2025, vol. 267, pp. 42366–42393.","short":"S.A. Maddipatla, N.E. Sellam, M.I. Bojan, S. Vedula, P. Schanda, A. Marx, A.M. Bronstein, in:, Proceedings of the 42nd International Conference on Machine Learning, ML Research Press, 2025, pp. 42366–42393.","ama":"Maddipatla SA, Sellam NE, Bojan MI, et al. Inverse problems with experiment-guided AlphaFold. In: <i>Proceedings of the 42nd International Conference on Machine Learning</i>. Vol 267. ML Research Press; 2025:42366-42393.","apa":"Maddipatla, S. A., Sellam, N. E., Bojan, M. I., Vedula, S., Schanda, P., Marx, A., &#38; Bronstein, A. M. (2025). Inverse problems with experiment-guided AlphaFold. In <i>Proceedings of the 42nd International Conference on Machine Learning</i> (Vol. 267, pp. 42366–42393). Vancouver, Canada: ML Research Press.","mla":"Maddipatla, Sai A., et al. “Inverse Problems with Experiment-Guided AlphaFold.” <i>Proceedings of the 42nd International Conference on Machine Learning</i>, vol. 267, ML Research Press, 2025, pp. 42366–93."},"alternative_title":["PMLR"],"project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"},{"_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0","name":"Structure and mechanism of the mitochondrial MIM insertase","grant_number":"I06223"}],"page":"42366 - 42393","type":"conference","status":"public","has_accepted_license":"1","ddc":["000","540"],"date_updated":"2026-02-19T08:56:43Z","day":"30","quality_controlled":"1","OA_type":"gold","conference":{"start_date":"2025-07-13","name":"ICML: International Conference on Machine Learning","end_date":"2025-07-19","location":"Vancouver, Canada"},"acknowledgement":"This work was supported by the Israeli Science Foundation (ISF) grant number 1834/24. We acknowledge support from the Austrian Science Fund (FWF, grant numbers I5812-B and I6223) and the financial support of the Helmsley Fellowships Program for Sustainability and Health. This research uses resources of the Institute of Science and Technology Austria’s scientific computing cluster. ","year":"2025","file":[{"date_updated":"2026-02-19T08:56:10Z","creator":"dernst","file_name":"2025_ICML_Maddipatla.pdf","relation":"main_file","content_type":"application/pdf","success":1,"checksum":"f33230a6d59b7978d4cd72795e4e9059","date_created":"2026-02-19T08:56:10Z","access_level":"open_access","file_id":"21338","file_size":1924177}],"department":[{"_id":"PaSc"},{"_id":"AlBr"},{"_id":"GradSch"}],"arxiv":1},{"volume":147,"month":"02","date_published":"2025-02-16T00:00:00Z","_id":"19072","publisher":"American Chemical Society","article_type":"original","title":"Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques","external_id":{"pmid":["39955787"],"isi":["001423628600001"]},"author":[{"last_name":"Lends","first_name":"Alons","full_name":"Lends, Alons"},{"last_name":"Lamon","full_name":"Lamon, Gaelle","first_name":"Gaelle"},{"full_name":"Delcourte, Loic","first_name":"Loic","last_name":"Delcourte"},{"last_name":"Sturny-Leclere","first_name":"Aude","full_name":"Sturny-Leclere, Aude"},{"last_name":"Grélard","first_name":"Axelle","full_name":"Grélard, Axelle"},{"full_name":"Morvan, Estelle","first_name":"Estelle","last_name":"Morvan"},{"last_name":"Abdul-Shukkoor","full_name":"Abdul-Shukkoor, Muhammed Bilal","first_name":"Muhammed Bilal"},{"first_name":"Mélanie","full_name":"Berbon, Mélanie","last_name":"Berbon"},{"first_name":"Alicia","full_name":"Vallet, Alicia","last_name":"Vallet"},{"first_name":"Birgit","full_name":"Habenstein, Birgit","last_name":"Habenstein"},{"last_name":"Dufourc","full_name":"Dufourc, Erick J.","first_name":"Erick J."},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul"},{"last_name":"Aimanianda","full_name":"Aimanianda, Vishukumar","first_name":"Vishukumar"},{"first_name":"Antoine","full_name":"Loquet, Antoine","last_name":"Loquet"}],"abstract":[{"text":"Pathogenic fungal and bacterial cells are enveloped within a cell wall, a molecular barrier at their cell surface, and a critical architecture that constantly evolves during pathogenesis. Understanding the molecular composition, structural organization, and mobility of polysaccharides constituting this cell envelope is crucial to correlate cell wall organization with its role in pathogenicity and to identify potential antifungal targets. For the fungal pathogen Cryptococcus neoformans, the characterization of the cell envelope has been complexified by the presence of an additional external polysaccharide capsular shell. Here, we investigate how magic-angle spinning (MAS) solid-state NMR techniques increase the analytical capabilities to characterize the structure and dynamics of this encapsulated pathogen. The versatility of proton detection experiments, dynamic-based filters, and relaxation measurements facilitate the discrimination of the highly mobile external capsular structure from the internal rigid cell wall of C. neoformans. In addition, we report the in situ detection of triglyceride molecules from lipid droplets based on NMR dynamic filters. Together, we demonstrate a nondestructive technique to study the cell wall architecture of encapsulated microbes using C. neoformans as a model, an airborne opportunistic fungal pathogen that infects mainly immunocompromised but also competent hosts.","lang":"eng"}],"oa_version":"None","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"publication_status":"published","article_processing_charge":"No","doi":"10.1021/jacs.4c16975","date_created":"2025-02-23T23:01:56Z","publication":"Journal of the American Chemical Society","intvolume":"       147","citation":{"mla":"Lends, Alons, et al. “Molecular Distinction of Cell Wall and Capsular Polysaccharides in Encapsulated Pathogens by in Situ Magic-Angle Spinning NMR Techniques.” <i>Journal of the American Chemical Society</i>, vol. 147, no. 8, American Chemical Society, 2025, pp. 6813–24, doi:<a href=\"https://doi.org/10.1021/jacs.4c16975\">10.1021/jacs.4c16975</a>.","apa":"Lends, A., Lamon, G., Delcourte, L., Sturny-Leclere, A., Grélard, A., Morvan, E., … Loquet, A. (2025). Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.4c16975\">https://doi.org/10.1021/jacs.4c16975</a>","chicago":"Lends, Alons, Gaelle Lamon, Loic Delcourte, Aude Sturny-Leclere, Axelle Grélard, Estelle Morvan, Muhammed Bilal Abdul-Shukkoor, et al. “Molecular Distinction of Cell Wall and Capsular Polysaccharides in Encapsulated Pathogens by in Situ Magic-Angle Spinning NMR Techniques.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2025. <a href=\"https://doi.org/10.1021/jacs.4c16975\">https://doi.org/10.1021/jacs.4c16975</a>.","ista":"Lends A, Lamon G, Delcourte L, Sturny-Leclere A, Grélard A, Morvan E, Abdul-Shukkoor MB, Berbon M, Vallet A, Habenstein B, Dufourc EJ, Schanda P, Aimanianda V, Loquet A. 2025. Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques. Journal of the American Chemical Society. 147(8), 6813–6824.","ieee":"A. Lends <i>et al.</i>, “Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques,” <i>Journal of the American Chemical Society</i>, vol. 147, no. 8. American Chemical Society, pp. 6813–6824, 2025.","short":"A. Lends, G. Lamon, L. Delcourte, A. Sturny-Leclere, A. Grélard, E. Morvan, M.B. Abdul-Shukkoor, M. Berbon, A. Vallet, B. Habenstein, E.J. Dufourc, P. Schanda, V. Aimanianda, A. Loquet, Journal of the American Chemical Society 147 (2025) 6813–6824.","ama":"Lends A, Lamon G, Delcourte L, et al. Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques. <i>Journal of the American Chemical Society</i>. 2025;147(8):6813-6824. doi:<a href=\"https://doi.org/10.1021/jacs.4c16975\">10.1021/jacs.4c16975</a>"},"isi":1,"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","language":[{"iso":"eng"}],"type":"journal_article","status":"public","issue":"8","page":"6813-6824","date_updated":"2025-09-30T10:36:53Z","day":"16","fulldoi":"https://doi.org/10.1021/jacs.4c16975","pmid":1,"scopus_import":"1","acknowledgement":"We thank the ANR (ANR-16-CE11-0020-02 to A. Loquet, and V.A. and ANR-21-CE17-0032-01 grant FUNPOLYVAC to V.A.) as well as the Swiss National Science Foundation for early postdoc mobility project P2EZP2_184258 to A. Lends. This work has benefited from the Biophysical and Structural Chemistry Platform at Institut Européen de Chimie et Biologie IECB, Centre National de la Recherche Scientifique CNRS Unité d’Appui et de Recherche UAR 3033, INSERM US001, and CNRS (IR-RMN FR3050 and Infranalytics FR2054).","quality_controlled":"1","OA_type":"closed access","year":"2025","department":[{"_id":"PaSc"}]},{"acknowledged_ssus":[{"_id":"NMR"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"month":"04","volume":31,"oa":1,"OA_place":"publisher","date_published":"2025-04-25T00:00:00Z","_id":"19555","publisher":"Wiley","article_type":"original","title":"Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy","external_id":{"pmid":["40080421"],"isi":["001479486400019"]},"author":[{"id":"81dc668a-19fa-11f0-bf31-d56534059ef3","first_name":"Darja","full_name":"Rohden, Darja","last_name":"Rohden"},{"last_name":"Toscano","full_name":"Toscano, Giorgia","first_name":"Giorgia"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"},{"last_name":"Lichtenecker","first_name":"Roman J.","full_name":"Lichtenecker, Roman J."}],"abstract":[{"text":"The charged arginine side chain is unique in determining many innate properties of proteins, contributing to stability and interaction surfaces, and directing allosteric regulation and enzymatic catalysis. NMR experiments can be used to reveal these processes at the molecular level, but it often requires selective insertion of carbon-13, nitrogen-15, and deuterium at defined atomic positions. We introduce a method to endow arginine residues with defined isotope patterns, combining synthetic organic chemistry and cell-based protein overexpression. The resulting proteins feature NMR active spin systems with optimized relaxation pathways leading to simplified NMR spectra with a sensitive response to changes in the chemical environment of the nuclei observed.","lang":"eng"}],"file_date_updated":"2025-08-05T12:59:24Z","article_number":"e202500408","publication_identifier":{"eissn":["1521-3765"],"issn":["0947-6539"]},"oa_version":"Published Version","doi":"10.1002/chem.202500408","publication_status":"published","article_processing_charge":"Yes (in subscription journal)","date_created":"2025-04-13T22:01:19Z","publication":"Chemistry - A European Journal","intvolume":"        31","citation":{"apa":"Rohden, D., Toscano, G., Schanda, P., &#38; Lichtenecker, R. J. (2025). Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. <i>Chemistry - A European Journal</i>. Wiley. <a href=\"https://doi.org/10.1002/chem.202500408\">https://doi.org/10.1002/chem.202500408</a>","mla":"Rohden, Darja, et al. “Synthesis of Selectively 13C/2H/15N- Labeled Arginine to Probe Protein Conformation and Interaction by NMR Spectroscopy.” <i>Chemistry - A European Journal</i>, vol. 31, no. 24, e202500408, Wiley, 2025, doi:<a href=\"https://doi.org/10.1002/chem.202500408\">10.1002/chem.202500408</a>.","ama":"Rohden D, Toscano G, Schanda P, Lichtenecker RJ. Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. <i>Chemistry - A European Journal</i>. 2025;31(24). doi:<a href=\"https://doi.org/10.1002/chem.202500408\">10.1002/chem.202500408</a>","short":"D. Rohden, G. Toscano, P. Schanda, R.J. Lichtenecker, Chemistry - A European Journal 31 (2025).","chicago":"Rohden, Darja, Giorgia Toscano, Paul Schanda, and Roman J. Lichtenecker. “Synthesis of Selectively 13C/2H/15N- Labeled Arginine to Probe Protein Conformation and Interaction by NMR Spectroscopy.” <i>Chemistry - A European Journal</i>. Wiley, 2025. <a href=\"https://doi.org/10.1002/chem.202500408\">https://doi.org/10.1002/chem.202500408</a>.","ieee":"D. Rohden, G. Toscano, P. Schanda, and R. J. Lichtenecker, “Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy,” <i>Chemistry - A European Journal</i>, vol. 31, no. 24. Wiley, 2025.","ista":"Rohden D, Toscano G, Schanda P, Lichtenecker RJ. 2025. Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. Chemistry - A European Journal. 31(24), e202500408."},"isi":1,"corr_author":"1","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","language":[{"iso":"eng"}],"type":"journal_article","status":"public","has_accepted_license":"1","project":[{"grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"issue":"24","date_updated":"2025-09-30T11:35:05Z","day":"25","pmid":1,"fulldoi":"https://doi.org/10.1002/chem.202500408","scopus_import":"1","ddc":["540"],"acknowledgement":"We thank Lea Marie Becker for assistance with python scripts used to analyze the labeling efficiency, and Undina Guillerm, Rajkumar Singh, and Anna Kapitonova for help with protein production. This work was supported by the Austrian Science Fund (FWF; project number I5812-B) through a French-Austrian bi-national research project. We thank the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the NMR Facility, as well as the NMR center and MS center of the University of Vienna.","quality_controlled":"1","OA_type":"hybrid","year":"2025","PlanS_conform":"1","file":[{"creator":"dernst","content_type":"application/pdf","file_name":"2025_ChemistryEur_Rohden.pdf","relation":"main_file","date_updated":"2025-08-05T12:59:24Z","access_level":"open_access","file_id":"20136","date_created":"2025-08-05T12:59:24Z","checksum":"e3788628644b5aac666cf079b05f8fa7","file_size":2840681,"success":1}],"department":[{"_id":"PaSc"}]},{"doi":"10.15479/AT-ISTA-19696","article_processing_charge":"No","date_created":"2025-05-14T10:46:07Z","oa_version":"Published Version","file_date_updated":"2025-07-31T08:14:40Z","author":[{"last_name":"Tatman","full_name":"Tatman, Benjamin","first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f"}],"department":[{"_id":"PaSc"}],"related_material":{"link":[{"relation":"research_paper","url":"http.//doi.org/10.1021/jacs.5c09057","description":"Paper to which the dataset corresponds."}],"record":[{"id":"20321","status":"public","relation":"research_data"}]},"year":"2025","corr_author":"1","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","file":[{"content_type":"application/zip","file_name":"dataset.zip","relation":"main_file","creator":"btatman","date_updated":"2025-07-31T08:14:40Z","file_size":557878455,"date_created":"2025-07-31T08:14:40Z","access_level":"open_access","file_id":"20094","checksum":"4c2d29404e070bda7d5619f728ec555c","success":1},{"content_type":"text/plain","relation":"main_file","file_name":"readme.txt","creator":"btatman","date_updated":"2025-07-31T08:14:21Z","file_size":3514,"access_level":"open_access","file_id":"20095","date_created":"2025-07-31T08:14:21Z","checksum":"6cbccd602be0ecb6ddb1f81fdfcadf92","success":1}],"citation":{"apa":"Tatman, B. (2025). Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-19696\">https://doi.org/10.15479/AT-ISTA-19696</a>","mla":"Tatman, Benjamin. <i>Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.”</i> Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19696\">10.15479/AT-ISTA-19696</a>.","short":"B. Tatman, (2025).","ama":"Tatman B. Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19696\">10.15479/AT-ISTA-19696</a>","ieee":"B. Tatman, “Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.’” Institute of Science and Technology Austria, 2025.","chicago":"Tatman, Benjamin. “Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.’” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-19696\">https://doi.org/10.15479/AT-ISTA-19696</a>.","ista":"Tatman B. 2025. Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-19696\">10.15479/AT-ISTA-19696</a>."},"oa":1,"date_published":"2025-07-31T00:00:00Z","month":"07","tmp":{"short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"status":"public","has_accepted_license":"1","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"type":"research_data","license":"https://creativecommons.org/licenses/by-nc-sa/4.0/","title":"Dataset for \"Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State\"","publisher":"Institute of Science and Technology Austria","_id":"19696","day":"31","date_updated":"2026-06-10T08:33:41Z","fulldoi":"https://doi.org/10.15479/AT-ISTA-19696","contributor":[{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","contributor_type":"project_leader","last_name":"Schanda"},{"first_name":"Vidhyalakshmi","contributor_type":"researcher","last_name":"Sridharan"},{"contributor_type":"researcher","last_name":"Uttarkabat","first_name":"Motilal"},{"first_name":"Christopher","contributor_type":"researcher","last_name":"Jaroniec"},{"first_name":"Matthias","contributor_type":"researcher","last_name":"Ernst"},{"contributor_type":"researcher","last_name":"Rovo","orcid":"0000-0001-8729-7326","id":"c316e53f-b965-11eb-b128-bb26acc59c00","first_name":"Petra"}]},{"publication":"Communications Biology","citation":{"chicago":"Castell, Sofía D., Consuelo M. Fernandez, Ignacio N. Tumas, Lucía M. Margara, Maria C Miserendino, Danilo G. Ceschin, Roberto J. Pezza, and Mariela R. Monti. “The Low-Fidelity DNA Pol IV Accelerates Evolution of Pathogenicity Genes in Pseudomonas Aeruginosa.” <i>Communications Biology</i>. Springer Nature, 2025. <a href=\"https://doi.org/10.1038/s42003-025-08589-5\">https://doi.org/10.1038/s42003-025-08589-5</a>.","ista":"Castell SD, Fernandez CM, Tumas IN, Margara LM, Miserendino MC, Ceschin DG, Pezza RJ, Monti MR. 2025. The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa. Communications Biology. 8, 1148.","ieee":"S. D. Castell <i>et al.</i>, “The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa,” <i>Communications Biology</i>, vol. 8. Springer Nature, 2025.","short":"S.D. Castell, C.M. Fernandez, I.N. Tumas, L.M. Margara, M.C. Miserendino, D.G. Ceschin, R.J. Pezza, M.R. Monti, Communications Biology 8 (2025).","ama":"Castell SD, Fernandez CM, Tumas IN, et al. The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa. <i>Communications Biology</i>. 2025;8. doi:<a href=\"https://doi.org/10.1038/s42003-025-08589-5\">10.1038/s42003-025-08589-5</a>","apa":"Castell, S. D., Fernandez, C. M., Tumas, I. N., Margara, L. M., Miserendino, M. C., Ceschin, D. G., … Monti, M. R. (2025). The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa. <i>Communications Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s42003-025-08589-5\">https://doi.org/10.1038/s42003-025-08589-5</a>","mla":"Castell, Sofía D., et al. “The Low-Fidelity DNA Pol IV Accelerates Evolution of Pathogenicity Genes in Pseudomonas Aeruginosa.” <i>Communications Biology</i>, vol. 8, 1148, Springer Nature, 2025, doi:<a href=\"https://doi.org/10.1038/s42003-025-08589-5\">10.1038/s42003-025-08589-5</a>."},"intvolume":"         8","isi":1,"DOAJ_listed":"1","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","language":[{"iso":"eng"}],"external_id":{"isi":["001541878500001"],"pmid":["40753298"]},"abstract":[{"text":"Specialized DNA polymerases facilitate various cellular processes. Despite extensive research, the mutagenic effects of these error-prone enzymes on genomes are not fully understood. Here we show that Pol IV promotes genomic instability in Pseudomonas aeruginosa by misincorporating oxidized guanine nucleotides. This activity led to a distinctive mutational signature, characterized by A-to-C transversions occurring preferentially at AT sites flanked by a 5’G and/or 3’C. Furthermore, Pol IV preferentially targeted pathogenicity genes located at specific chromosomal locations near the replication termination region and rRNA-encoding operons. Half of the mutation events catalyzed by Pol IV impaired gene function. This can be attributed to the bias of Pol IV for mutating codons with its preferred sequence contexts, leading to substitutions to unreactive alanine and glycine residues. Remarkably, mutation signatures identified for Pol IV were found in clinical isolate genomes of P. aeruginosa, providing compelling evidence for its role in genetic diversification during pathogen adaptation.","lang":"eng"}],"author":[{"last_name":"Castell","first_name":"Sofía D.","full_name":"Castell, Sofía D."},{"first_name":"Consuelo M.","full_name":"Fernandez, Consuelo M.","last_name":"Fernandez"},{"last_name":"Tumas","full_name":"Tumas, Ignacio N.","first_name":"Ignacio N."},{"full_name":"Margara, Lucía M.","first_name":"Lucía M.","last_name":"Margara"},{"full_name":"Miserendino, Maria C","first_name":"Maria C","id":"273e0cbd-72f0-11ef-b75a-f9f932e292fa","last_name":"Miserendino"},{"first_name":"Danilo G.","full_name":"Ceschin, Danilo G.","last_name":"Ceschin"},{"last_name":"Pezza","full_name":"Pezza, Roberto J.","first_name":"Roberto J."},{"full_name":"Monti, Mariela R.","first_name":"Mariela R.","last_name":"Monti"}],"article_number":"1148","publication_identifier":{"eissn":["2399-3642"]},"oa_version":"Published Version","article_processing_charge":"Yes","date_created":"2025-08-17T22:01:35Z","doi":"10.1038/s42003-025-08589-5","publication_status":"published","_id":"20184","publisher":"Springer Nature","article_type":"original","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s42003-025-08589-5"}],"title":"The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)"},"volume":8,"month":"08","oa":1,"OA_place":"publisher","date_published":"2025-08-02T00:00:00Z","year":"2025","PlanS_conform":"1","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"acknowledgement":"This work was supported by the Secretaría de Ciencia y Técnica (33620230100926CB), Universidad Nacional de Córdoba; and the Agencia Nacional de Promoción Científica y Técnica (PICT 2018-4527).\r\n\r\n","quality_controlled":"1","OA_type":"gold","day":"02","date_updated":"2025-09-30T14:18:46Z","fulldoi":"https://doi.org/10.1038/s42003-025-08589-5","pmid":1,"scopus_import":"1","ddc":["570"],"type":"journal_article","status":"public","has_accepted_license":"1"},{"title":"Data of: \"Quantifying the carbon footprint of conference travel: the case of NMR meetings\"","contributor":[{"first_name":"Natalia","id":"D2761128-D73D-11E9-A1BF-BA0DE6697425","last_name":"Ruzickova","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Kapoor","id":"84b9700b-15b2-11ec-abd3-831089e67615","first_name":"Lucky"},{"contributor_type":"researcher","last_name":"Leitner","id":"4c665ce3-0016-11ec-bea0-e44de7a4fa3d","first_name":"Valentin"},{"last_name":"Zivadinovic","contributor_type":"researcher","first_name":"Predrag","id":"68AA0E5A-AFDA-11E9-9994-141DE6697425"},{"last_name":"Sisak","contributor_type":"researcher","first_name":"Maria A","id":"44A03D04-AEA4-11E9-B225-EA2DE6697425"},{"contributor_type":"researcher","last_name":"Mweka","id":"2a69ab4b-896a-11ed-bdf8-cb8641cf2b21","first_name":"Cecelia N"},{"last_name":"Dobbelaere","contributor_type":"supervisor","first_name":"Jeroen A","id":"c15a5412-de82-11ed-b809-8dc1aa996e40"},{"first_name":"Georgios","orcid":"0000-0001-8342-202X","id":"38DB5788-F248-11E8-B48F-1D18A9856A87","last_name":"Katsaros","contributor_type":"supervisor"}],"fulldoi":"https://doi.org/10.15479/AT-ISTA-20242","date_updated":"2026-06-10T08:45:12Z","_id":"20242","publisher":"Institute of Science and Technology Austria","month":"09","date_published":"2025-09-01T00:00:00Z","oa":1,"type":"research_data","has_accepted_license":"1","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","image":"/images/cc_by_nc.png","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"status":"public","file":[{"success":1,"file_size":42368943,"checksum":"055044b03f835cb98c45d0504f1db96e","file_id":"20244","date_created":"2025-08-31T15:09:44Z","access_level":"open_access","date_updated":"2025-08-31T15:09:44Z","relation":"main_file","file_name":"Abstracts.zip","content_type":"application/zip","creator":"pschanda"},{"creator":"pschanda","relation":"main_file","file_name":"data_CO2_conferences.zip","content_type":"application/zip","date_updated":"2025-08-31T15:11:58Z","checksum":"1492683af736ac65088b77e12b52c3b0","access_level":"open_access","date_created":"2025-08-31T15:11:58Z","file_id":"20245","file_size":470659,"success":1},{"date_updated":"2025-08-31T15:12:03Z","file_name":"Figure6_predictions.zip","relation":"main_file","content_type":"application/zip","creator":"pschanda","success":1,"file_size":1138772,"checksum":"8ac69071f7508e77b5ca91fa5018339a","access_level":"open_access","file_id":"20246","date_created":"2025-08-31T15:12:03Z"},{"creator":"pschanda","relation":"main_file","file_name":"ExcelFileAnalysisCode.py","content_type":"text/x-python-script","date_updated":"2025-08-31T15:12:07Z","checksum":"19b77db247feecdc36fbe6f68d94a76d","access_level":"open_access","date_created":"2025-08-31T15:12:07Z","file_id":"20247","file_size":6558,"success":1},{"checksum":"39655e28c6df523f4f9662dc58c94623","date_created":"2025-08-31T15:12:11Z","access_level":"open_access","file_id":"20248","file_size":1107467,"success":1,"creator":"pschanda","file_name":"emissions_spectrometers_and_Parisgoal.pdf","relation":"main_file","content_type":"application/pdf","date_updated":"2025-08-31T15:12:11Z"},{"success":1,"checksum":"2e9a9460b3f2abe7e46179561a63492b","file_id":"20263","access_level":"open_access","date_created":"2025-09-01T11:05:27Z","file_size":3994,"date_updated":"2025-09-01T11:05:27Z","creator":"pschanda","relation":"main_file","file_name":"README","content_type":"application/octet-stream"}],"corr_author":"1","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","year":"2025","department":[{"_id":"PaSc"}],"related_material":{"record":[{"relation":"used_in_publication","id":"20664","status":"public"}]},"citation":{"ista":"Schanda P. 2025. Data of: ‘Quantifying the carbon footprint of conference travel: the case of NMR meetings’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-20242\">10.15479/AT-ISTA-20242</a>.","ieee":"P. Schanda, “Data of: ‘Quantifying the carbon footprint of conference travel: the case of NMR meetings.’” Institute of Science and Technology Austria, 2025.","chicago":"Schanda, Paul. “Data of: ‘Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.’” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-20242\">https://doi.org/10.15479/AT-ISTA-20242</a>.","short":"P. Schanda, (2025).","ama":"Schanda P. Data of: “Quantifying the carbon footprint of conference travel: the case of NMR meetings.” 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20242\">10.15479/AT-ISTA-20242</a>","apa":"Schanda, P. (2025). Data of: “Quantifying the carbon footprint of conference travel: the case of NMR meetings.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-20242\">https://doi.org/10.15479/AT-ISTA-20242</a>","mla":"Schanda, Paul. <i>Data of: “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.”</i> Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20242\">10.15479/AT-ISTA-20242</a>."},"keyword":["sustainability","conference travel"],"oa_version":"Published Version","doi":"10.15479/AT-ISTA-20242","date_created":"2025-08-31T15:14:18Z","article_processing_charge":"No","abstract":[{"lang":"eng","text":"This repository contains calculations of carbon footprints of NMR conferences, as described in the article by \r\nLucky N. Kapoor, Natalia Ruzickova, Predrag Živadinović, Valentin Leitner, Maria Anna Sisak, Cecelia Mweka, Jeroen Dobbelaere, Georgios Katsaros, and Paul Schanda\r\nPublished in Magnetic Resonance, 2025."}],"author":[{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"}],"file_date_updated":"2025-09-01T11:05:27Z"},{"year":"2025","PlanS_conform":"1","file":[{"date_updated":"2025-09-10T07:53:10Z","content_type":"application/pdf","file_name":"2025_JACS_Tatman.pdf","relation":"main_file","creator":"dernst","success":1,"file_size":5235353,"access_level":"open_access","file_id":"20337","date_created":"2025-09-10T07:53:10Z","checksum":"b350d56ddddefea96cebd62c277c0ff5"}],"department":[{"_id":"PaSc"},{"_id":"NMR"}],"quality_controlled":"1","OA_type":"hybrid","acknowledgement":"The authors thank Alexey Krushelnitsky for useful discussions. C.P.J. thanks NSF (MCB-2303862) and NIH (R35GM156238 and S10OD012303) for funding. This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities.","scopus_import":"1","ddc":["540"],"day":"01","date_updated":"2026-06-10T08:33:41Z","fulldoi":"https://doi.org/10.1021/jacs.5c09057","pmid":1,"page":"29315-29326","issue":"32","type":"journal_article","status":"public","has_accepted_license":"1","isi":1,"corr_author":"1","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","language":[{"iso":"eng"}],"related_material":{"record":[{"relation":"used_in_publication","status":"public","id":"19696"}]},"publication":"Journal of the American Chemical Society","citation":{"apa":"Tatman, B., Sridharan, V., Uttarkabat, M., Jaroniec, C. P., Ernst, M., Rovo, P., &#38; Schanda, P. (2025). Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.5c09057\">https://doi.org/10.1021/jacs.5c09057</a>","mla":"Tatman, Benjamin, et al. “Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” <i>Journal of the American Chemical Society</i>, vol. 147, no. 32, American Chemical Society, 2025, pp. 29315–26, doi:<a href=\"https://doi.org/10.1021/jacs.5c09057\">10.1021/jacs.5c09057</a>.","chicago":"Tatman, Benjamin, Vidhyalakshmi Sridharan, Motilal Uttarkabat, Christopher P. Jaroniec, Matthias Ernst, Petra Rovo, and Paul Schanda. “Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2025. <a href=\"https://doi.org/10.1021/jacs.5c09057\">https://doi.org/10.1021/jacs.5c09057</a>.","ieee":"B. Tatman <i>et al.</i>, “Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR,” <i>Journal of the American Chemical Society</i>, vol. 147, no. 32. American Chemical Society, pp. 29315–29326, 2025.","ista":"Tatman B, Sridharan V, Uttarkabat M, Jaroniec CP, Ernst M, Rovo P, Schanda P. 2025. Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. Journal of the American Chemical Society. 147(32), 29315–29326.","short":"B. Tatman, V. Sridharan, M. Uttarkabat, C.P. Jaroniec, M. Ernst, P. Rovo, P. Schanda, Journal of the American Chemical Society 147 (2025) 29315–29326.","ama":"Tatman B, Sridharan V, Uttarkabat M, et al. Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. <i>Journal of the American Chemical Society</i>. 2025;147(32):29315-29326. doi:<a href=\"https://doi.org/10.1021/jacs.5c09057\">10.1021/jacs.5c09057</a>"},"intvolume":"       147","oa_version":"Published Version","publication_identifier":{"eissn":["1520-5126"],"issn":["0002-7863"]},"doi":"10.1021/jacs.5c09057","article_processing_charge":"Yes (via OA deal)","publication_status":"published","date_created":"2025-09-10T05:37:19Z","external_id":{"pmid":["40748291"],"isi":["001542746200001"]},"abstract":[{"lang":"eng","text":"Microsecond-to-millisecond motions are instrumental for many biomolecular functions, including enzymatic activity and ligand binding. Bloch-McConnell Relaxation Dispersion (BMRD) Nuclear Magnetic Resonance (NMR) spectroscopy is a key technique for studying these dynamic processes. While BMRD experiments are routinely used to probe protein motions in solution, the experiment is more demanding in the solid state, where dipolar couplings complicate the spin dynamics. It is believed that high deuteration levels are required and sufficient to obtain accurate and quantitative data. Here we show that even under fast magic-angle spinning and high levels of deuteration artifactual “bumps” in 15N R1ρ BMRD profiles are common. The origin of these artifacts is identified as a second-order three-spin Mixed Rotational and Rotary Resonance (MIRROR) recoupling condition. These artifacts are found to be a significant confounding factor for the accurate quantification of microsecond protein dynamics using BMRD in the solid state. We show that the application of low-power continuous wave (CW) decoupling simultaneously with the 15N spin-lock leads to the suppression of these conditions and enables quantitative measurements of microsecond exchange in the solid state. Remarkably, the application of decoupling allows the measurement of accurate BMRD even in fully protonated proteins at 100 kHz MAS, thus extending the scope of μs dynamics measurements in MAS NMR."}],"author":[{"id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin","first_name":"Benjamin","last_name":"Tatman"},{"full_name":"Sridharan, Vidhyalakshmi","first_name":"Vidhyalakshmi","last_name":"Sridharan"},{"full_name":"Uttarkabat, Motilal","first_name":"Motilal","last_name":"Uttarkabat"},{"first_name":"Christopher P.","full_name":"Jaroniec, Christopher P.","last_name":"Jaroniec"},{"last_name":"Ernst","full_name":"Ernst, Matthias","first_name":"Matthias"},{"id":"c316e53f-b965-11eb-b128-bb26acc59c00","orcid":"0000-0001-8729-7326","full_name":"Rovo, Petra","first_name":"Petra","last_name":"Rovo"},{"first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda"}],"file_date_updated":"2025-09-10T07:53:10Z","article_type":"original","title":"Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR","_id":"20321","publisher":"American Chemical Society","volume":147,"month":"08","oa":1,"OA_place":"publisher","date_published":"2025-08-01T00:00:00Z","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"}},{"department":[{"_id":"JoFi"},{"_id":"GaTk"},{"_id":"JoCs"},{"_id":"EvBe"},{"_id":"TaHa"},{"_id":"GradSch"},{"_id":"GeKa"},{"_id":"PaSc"}],"PlanS_conform":"1","file":[{"creator":"dernst","file_name":"2025_MagneticResonance_Kapoor.pdf","relation":"main_file","content_type":"application/pdf","date_updated":"2025-11-24T08:25:19Z","checksum":"c63dd47b0e77f9451821436bb77d27c9","date_created":"2025-11-24T08:25:19Z","file_id":"20672","access_level":"open_access","file_size":3081399,"success":1}],"year":"2025","acknowledgement":"First and foremost, we are grateful to the conference organizers who have provided data, either in the form of tables or by pointing us to abstract books. We thank the reviewers and the handling editor (Gottfried Otting) for the careful reading and suggestions. This project emerged from an interactive course about energy and climate, held at IST Austria by Jeroen Dobbelaere, Georgios Katsaros and Paul Schanda. We are grateful to ISTA's Graduate School for enabling this interdisciplinary course and to all participating students. We thank the following persons for discussions and/or comments about the manuscript: Helene Van Melckebeke, Mei Hong, Jeff Hoch, Gottfried Otting and Matthias Ernst. For the preparation of the manuscript, AI tools have been used, namely for finding relevant literature (ChatGPT) and for correcting the text (Writefull, within Overleaf LaTeX).","OA_type":"gold","quality_controlled":"1","fulldoi":"https://doi.org/10.5194/mr-6-243-2025","date_updated":"2026-06-10T08:45:11Z","day":"10","ddc":["000"],"scopus_import":"1","has_accepted_license":"1","APC_amount":"1260 EUR","status":"public","type":"journal_article","issue":"2","page":"243-256","project":[{"_id":"B67AFEDC-15C9-11EA-A837-991A96BB2854","name":"IST Austria Open Access Fund"}],"citation":{"short":"L. Kapoor, N. Ruzickova, P. Zivadinovic, V. Leitner, M.A. Sisak, C.N. Mweka, J.A. Dobbelaere, G. Katsaros, P. Schanda, Magnetic Resonance 6 (2025) 243–256.","ama":"Kapoor L, Ruzickova N, Zivadinovic P, et al. Quantifying the carbon footprint of conference travel: The case of NMR meetings. <i>Magnetic Resonance</i>. 2025;6(2):243-256. doi:<a href=\"https://doi.org/10.5194/mr-6-243-2025\">10.5194/mr-6-243-2025</a>","ieee":"L. Kapoor <i>et al.</i>, “Quantifying the carbon footprint of conference travel: The case of NMR meetings,” <i>Magnetic Resonance</i>, vol. 6, no. 2. Copernicus Publications, pp. 243–256, 2025.","ista":"Kapoor L, Ruzickova N, Zivadinovic P, Leitner V, Sisak MA, Mweka CN, Dobbelaere JA, Katsaros G, Schanda P. 2025. Quantifying the carbon footprint of conference travel: The case of NMR meetings. Magnetic Resonance. 6(2), 243–256.","chicago":"Kapoor, Lucky, Natalia Ruzickova, Predrag Zivadinovic, Valentin Leitner, Maria A Sisak, Cecelia N Mweka, Jeroen A Dobbelaere, Georgios Katsaros, and Paul Schanda. “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.” <i>Magnetic Resonance</i>. Copernicus Publications, 2025. <a href=\"https://doi.org/10.5194/mr-6-243-2025\">https://doi.org/10.5194/mr-6-243-2025</a>.","apa":"Kapoor, L., Ruzickova, N., Zivadinovic, P., Leitner, V., Sisak, M. A., Mweka, C. N., … Schanda, P. (2025). Quantifying the carbon footprint of conference travel: The case of NMR meetings. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-6-243-2025\">https://doi.org/10.5194/mr-6-243-2025</a>","mla":"Kapoor, Lucky, et al. “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.” <i>Magnetic Resonance</i>, vol. 6, no. 2, Copernicus Publications, 2025, pp. 243–56, doi:<a href=\"https://doi.org/10.5194/mr-6-243-2025\">10.5194/mr-6-243-2025</a>."},"intvolume":"         6","publication":"Magnetic Resonance","related_material":{"link":[{"relation":"research_data","url":"https://ista.ac.at/en/news/carbon-footprint-of-conference-travel/","description":"News on ISTA website"}],"record":[{"status":"public","id":"20242","relation":"research_data"}]},"language":[{"iso":"eng"}],"corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","DOAJ_listed":"1","file_date_updated":"2025-11-24T08:25:19Z","abstract":[{"text":"Conference travel contributes to the climate footprint of academic research. Here, we provide a quantitative estimate of the carbon emissions associated with conference attendance by analyzing travel data from participants of 10 international conferences in the field of magnetic resonance, namely EUROMAR, ENC and ICMRBS. We find that attending a EUROMAR conference produces, on average, more than 1 t CO2 eq.. For the analyzed conferences outside Europe, the corresponding value is about 2–3 times higher, on average, with intercontinental trips amounting to up to 5 t. We compare these conference-related emissions to other activities associated with research and show that conference travel is a substantial portion of the total climate footprint of a researcher in magnetic resonance. We explore several strategies to reduce these emissions, including the impact of selecting conference venues more strategically and the possibility of decentralized conferences. Through a detailed comparison of train versus air travel – accounting for both direct and infrastructure-related emissions – we demonstrate that train travel offers considerable carbon savings. These data may provide a basis for strategic choices of future conferences in the field and for individuals deciding on their conference attendance.","lang":"eng"}],"author":[{"last_name":"Kapoor","full_name":"Kapoor, Lucky","first_name":"Lucky","orcid":"0000-0001-8319-2148","id":"84b9700b-15b2-11ec-abd3-831089e67615"},{"first_name":"Natalia","full_name":"Ruzickova, Natalia","id":"D2761128-D73D-11E9-A1BF-BA0DE6697425","last_name":"Ruzickova"},{"id":"68AA0E5A-AFDA-11E9-9994-141DE6697425","first_name":"Predrag","full_name":"Zivadinovic, Predrag","last_name":"Zivadinovic"},{"last_name":"Leitner","id":"4c665ce3-0016-11ec-bea0-e44de7a4fa3d","full_name":"Leitner, Valentin","first_name":"Valentin"},{"last_name":"Sisak","full_name":"Sisak, Maria A","first_name":"Maria A","id":"44A03D04-AEA4-11E9-B225-EA2DE6697425"},{"id":"2a69ab4b-896a-11ed-bdf8-cb8641cf2b21","full_name":"Mweka, Cecelia N","first_name":"Cecelia N","last_name":"Mweka"},{"last_name":"Dobbelaere","id":"c15a5412-de82-11ed-b809-8dc1aa996e40","first_name":"Jeroen A","full_name":"Dobbelaere, Jeroen A"},{"orcid":"0000-0001-8342-202X","id":"38DB5788-F248-11E8-B48F-1D18A9856A87","first_name":"Georgios","full_name":"Katsaros, Georgios","last_name":"Katsaros"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"doi":"10.5194/mr-6-243-2025","article_processing_charge":"Yes","date_created":"2025-11-23T23:01:39Z","publication_status":"published","publication_identifier":{"eissn":["2699-0016"]},"oa_version":"Published Version","publisher":"Copernicus Publications","_id":"20664","title":"Quantifying the carbon footprint of conference travel: The case of NMR meetings","article_type":"original","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"OA_place":"publisher","date_published":"2025-11-10T00:00:00Z","oa":1,"volume":6,"month":"11"}]