[{"date_updated":"2026-06-10T09:28:41Z","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","day":"18","OA_type":"free access","corr_author":"1","has_accepted_license":"1","ddc":["541"],"contributor":[{"first_name":"Giorgia","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","contributor_type":"researcher","last_name":"Toscano"},{"last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna","contributor_type":"researcher"},{"last_name":"Singh","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20","first_name":"Rajkumar","contributor_type":"researcher"},{"id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","first_name":"Undina","contributor_type":"researcher","last_name":"Guillerm"},{"last_name":"Lichtenecker","first_name":"Roman","contributor_type":"researcher"}],"_id":"21284","author":[{"first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151"},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"publisher":"Institute of Science and Technology Austria","file_date_updated":"2026-02-17T10:11:14Z","oa":1,"date_published":"2026-02-18T00:00:00Z","type":"research_data","doi":"10.15479/AT-ISTA-21284","title":"Research data for \"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants\"","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.","year":"2026","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."}],"month":"2","article_processing_charge":"No","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"status":"public","file":[{"relation":"main_file","date_created":"2026-02-17T10:11:14Z","creator":"lbecker","file_id":"21285","access_level":"open_access","date_updated":"2026-02-17T10:11:14Z","file_name":"Research_data.zip","file_size":36996027,"content_type":"application/zip","success":1,"checksum":"2d3105f26be578073b88ee1f2ea0bdb1"},{"relation":"table_of_contents","creator":"lbecker","date_created":"2026-02-17T10:11:14Z","file_id":"21286","access_level":"open_access","date_updated":"2026-02-17T10:11:14Z","file_name":"README.txt","file_size":1993,"content_type":"text/plain","checksum":"e24aebcdb8856cb181cbaa02de020ddb"}],"oa_version":"Published Version","citation":{"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>.","short":"L.M. Becker, P. Schanda, (2026).","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>"},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"OA_place":"repository","date_created":"2026-02-17T10:17:14Z","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png"}},{"date_created":"2026-05-03T22:01:36Z","article_type":"original","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"oa_version":"Published Version","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"citation":{"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>","short":"L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker, P. Schanda, Magnetic Resonance 7 (2026) 29–37.","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.","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>.","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>."},"OA_place":"publisher","status":"public","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."}],"month":"04","volume":7,"article_processing_charge":"Yes","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"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).","issue":"1","intvolume":"         7","year":"2026","title":"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants","pmid":1,"publication_identifier":{"eissn":["2699-0016"]},"doi":"10.5194/mr-7-29-2026","date_published":"2026-04-16T00:00:00Z","language":[{"iso":"eng"}],"publication":"Magnetic Resonance","scopus_import":"1","type":"journal_article","oa":1,"ddc":["540"],"has_accepted_license":"1","_id":"21777","author":[{"last_name":"Becker","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie","first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79"},{"id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","first_name":"Giorgia","full_name":"Toscano, Giorgia","last_name":"Toscano"},{"last_name":"Kapitonova","full_name":"Kapitonova, Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna"},{"last_name":"Singh","full_name":"Singh, Rajkumar","first_name":"Rajkumar","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20"},{"first_name":"Undina","id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","last_name":"Guillerm","full_name":"Guillerm, Undina"},{"full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker","first_name":"Roman J."},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul"}],"publisher":"Copernicus Publications","DOAJ_listed":"1","publication_status":"published","PlanS_conform":"1","corr_author":"1","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","OA_type":"gold","external_id":{"pmid":["42057802"]},"day":"16","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"}],"date_updated":"2026-05-07T06:49:59Z","page":"29-37","main_file_link":[{"open_access":"1","url":"https://doi.org/10.5194/mr-7-29-2026"}]},{"article_processing_charge":"Yes (via OA deal)","month":"06","volume":35,"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"}],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"status":"public","oa_version":"Published Version","file":[{"checksum":"e0163459a7238fdcc3fc5e17bedcce9a","success":1,"content_type":"application/pdf","date_updated":"2026-06-02T07:23:12Z","file_name":"2026_ProteinScience_Schneider.pdf","file_size":3897305,"access_level":"open_access","file_id":"21937","creator":"dernst","date_created":"2026-06-02T07:23:12Z","relation":"main_file"}],"OA_place":"publisher","citation":{"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.","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>.","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>","short":"J. Schneider, U. Guillerm, C. Simoes Pereira, P. Schanda, Protein Science 35 (2026).","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>"},"article_type":"original","date_created":"2026-05-31T22:02:12Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"scopus_import":"1","date_published":"2026-06-01T00:00:00Z","publication":"Protein Science","language":[{"iso":"eng"}],"type":"journal_article","doi":"10.1002/pro.70630","title":"Dynamic disorder is crucial for mitochondrial protein import","publication_identifier":{"issn":["0961-8368"],"eissn":["1469-896X"]},"pmid":1,"article_number":"e70630","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.","issue":"6","year":"2026","intvolume":"        35","corr_author":"1","PlanS_conform":"1","quality_controlled":"1","publication_status":"published","_id":"21929","author":[{"first_name":"Jakob","id":"64368429-eb97-11eb-a6c2-c980b1f44415","last_name":"Schneider","full_name":"Schneider, Jakob"},{"id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","first_name":"Undina","full_name":"Guillerm, Undina","last_name":"Guillerm"},{"first_name":"Caroline","id":"87266c4a-96d2-11ef-be2c-fe5633233ec3","full_name":"Simoes Pereira, Caroline","last_name":"Simoes Pereira"},{"full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul"}],"ddc":["572"],"has_accepted_license":"1","publisher":"Wiley","oa":1,"file_date_updated":"2026-06-02T07:23:12Z","date_updated":"2026-06-02T07:26:34Z","project":[{"name":"Structure and mechanism of the mitochondrial MIM insertase","_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0","grant_number":"I06223"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","OA_type":"hybrid","external_id":{"pmid":["42159315"]},"day":"01"},{"date_updated":"2026-06-24T08:47:58Z","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41557-026-02155-0"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["42271006"]},"day":"10","OA_type":"hybrid","project":[{"grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0"}],"publication_status":"epub_ahead","researchdata_availability":"yes","PlanS_conform":"1","quality_controlled":"1","corr_author":"1","oa":1,"author":[{"id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie"},{"first_name":"Haohao","full_name":"Fu, Haohao","last_name":"Fu"},{"full_name":"Tatman, Benjamin","last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin"},{"first_name":"Matthias","full_name":"Dreydoppel, Matthias","last_name":"Dreydoppel"},{"full_name":"Kapitonova, Anna","last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna"},{"last_name":"Balazs","orcid":"0000-0001-7597-043X","full_name":"Balazs, Daniel","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","first_name":"Daniel"},{"full_name":"Weininger, Ulrich","last_name":"Weininger","first_name":"Ulrich"},{"full_name":"Engilberge, Sylvain","last_name":"Engilberge","first_name":"Sylvain"},{"first_name":"Christophe","full_name":"Chipot, Christophe","last_name":"Chipot"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606"}],"_id":"22105","ddc":["540"],"has_accepted_license":"1","publisher":"Springer Nature","doi":"10.1038/s41557-026-02155-0","scopus_import":"1","date_published":"2026-06-10T00:00:00Z","publication":"Nature Chemistry","language":[{"iso":"eng"}],"type":"journal_article","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).","year":"2026","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.","title":"Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes","publication_identifier":{"eissn":["17554349"],"issn":["17554330"]},"pmid":1,"related_material":{"record":[{"relation":"research_data","id":"20641","status":"public"},{"status":"public","id":"21145","relation":"research_data"}]},"status":"public","article_processing_charge":"Yes (via OA deal)","month":"06","abstract":[{"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.","lang":"eng"}],"department":[{"_id":"PaSc"},{"_id":"LifeSc"}],"article_type":"original","date_created":"2026-06-21T22:03:01Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"oa_version":"Published Version","das_tickbox":"1","OA_place":"publisher","supplementarymaterial":"yes","citation":{"ieee":"L. M. Becker <i>et al.</i>, “Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes,” <i>Nature Chemistry</i>. Springer Nature, 2026.","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.","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>.","mla":"Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>.","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>","short":"L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U. Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry (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. doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>"},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}]},{"oa_version":"Published Version","file":[{"access_level":"open_access","creator":"lbecker","date_created":"2026-02-05T13:52:37Z","relation":"table_of_contents","file_id":"21146","checksum":"02a419cce8cea450bc952f35488d2df5","content_type":"text/plain","file_size":4263,"file_name":"README.txt","date_updated":"2026-02-05T13:52:37Z"},{"creator":"lbecker","date_created":"2026-02-05T13:52:41Z","relation":"main_file","file_id":"21147","access_level":"open_access","content_type":"application/zip","file_size":50647107,"date_updated":"2026-02-05T13:52:41Z","file_name":"Research_Data.zip","success":1,"checksum":"b0b82b1aa73985b0b308a3fa52d21aea"}],"citation":{"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>.","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>.","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>","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.","short":"L.M. Becker, P. Schanda, C. Chipot, (2026).","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>"},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"date_created":"2026-02-05T13:54:39Z","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png"},"article_processing_charge":"No","month":"02","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. "}],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"related_material":{"record":[{"id":"20641","status":"public","relation":"earlier_version"},{"status":"public","id":"22105","relation":"used_in_publication"}]},"status":"public","title":"Additional Data for \"Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes\"","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.","year":"2026","date_published":"2026-02-09T00:00:00Z","type":"research_data","doi":"10.15479/AT-ISTA-21145","author":[{"first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","last_name":"Becker","full_name":"Becker, Lea Marie"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606"},{"full_name":"Chipot, Christophe","last_name":"Chipot","first_name":"Christophe"}],"_id":"21145","contributor":[{"contributor_type":"researcher","first_name":"Haohao","last_name":"Fu"},{"last_name":"Tatman","contributor_type":"researcher","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin"},{"first_name":"Matthias","contributor_type":"researcher","last_name":"Dreydoppel"},{"contributor_type":"researcher","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","last_name":"Kapitonova"},{"first_name":"Daniel","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","contributor_type":"researcher","orcid":"0000-0001-7597-043X","last_name":"Balazs"},{"contributor_type":"researcher","first_name":"Ulrich","last_name":"Weininger"},{"last_name":"Engilberge","first_name":"Sylvain","contributor_type":"researcher"}],"has_accepted_license":"1","ddc":["572"],"publisher":"Institute of Science and Technology Austria","oa":1,"file_date_updated":"2026-02-05T13:52:41Z","corr_author":"1","project":[{"grant_number":"26777","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"09","date_updated":"2026-06-24T08:47:57Z"},{"acknowledged_ssus":[{"_id":"ScienComp"}],"citation":{"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.","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.","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.","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.","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."},"alternative_title":["PMLR"],"OA_place":"publisher","file":[{"access_level":"open_access","relation":"main_file","date_created":"2026-02-19T08:56:10Z","creator":"dernst","file_id":"21338","success":1,"checksum":"f33230a6d59b7978d4cd72795e4e9059","file_name":"2025_ICML_Maddipatla.pdf","file_size":1924177,"date_updated":"2026-02-19T08:56:10Z","content_type":"application/pdf"}],"oa_version":"Published Version","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"date_created":"2026-02-18T12:11:17Z","department":[{"_id":"PaSc"},{"_id":"AlBr"},{"_id":"GradSch"}],"month":"07","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"}],"volume":267,"article_processing_charge":"No","status":"public","publication_identifier":{"eissn":["2640-3498"]},"arxiv":1,"title":"Inverse problems with experiment-guided AlphaFold","intvolume":"       267","year":"2025","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. ","type":"conference","date_published":"2025-07-30T00:00:00Z","language":[{"iso":"eng"}],"publication":"Proceedings of the 42nd International Conference on Machine Learning","publisher":"ML Research Press","ddc":["000","540"],"has_accepted_license":"1","_id":"21327","author":[{"id":"e957f5e5-91c9-11f0-a95f-e090f66ecb4d","first_name":"Sai A","full_name":"Maddipatla, Sai A","last_name":"Maddipatla"},{"first_name":"Nadav E","id":"ef280fe0-91c9-11f0-a95f-8dea3f5bc513","full_name":"Sellam, Nadav E","last_name":"Sellam"},{"full_name":"Bojan, Meital I","last_name":"Bojan","first_name":"Meital I","id":"11d88cf5-91ca-11f0-a95f-edf9f08f47b7"},{"id":"94f2fe44-70fa-11f0-b76b-92922c09452b","first_name":"Sanketh","full_name":"Vedula, Sanketh","last_name":"Vedula"},{"full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"last_name":"Marx","full_name":"Marx, Ailie","first_name":"Ailie"},{"first_name":"Alexander","id":"58f3726e-7cba-11ef-ad8b-e6e8cb3904e6","full_name":"Bronstein, Alexander","orcid":"0000-0001-9699-8730","last_name":"Bronstein"}],"conference":{"end_date":"2025-07-19","location":"Vancouver, Canada","name":"ICML: International Conference on Machine Learning","start_date":"2025-07-13"},"file_date_updated":"2026-02-19T08:56:10Z","oa":1,"corr_author":"1","quality_controlled":"1","publication_status":"published","project":[{"grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery"},{"name":"Structure and mechanism of the mitochondrial MIM insertase","_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0","grant_number":"I06223"}],"OA_type":"gold","day":"30","external_id":{"arxiv":["2502.09372"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"42366 - 42393","date_updated":"2026-02-19T08:56:43Z"},{"title":"Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques","pmid":1,"publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"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).","issue":"8","year":"2025","intvolume":"       147","scopus_import":"1","date_published":"2025-02-16T00:00:00Z","publication":"Journal of the American Chemical Society","language":[{"iso":"eng"}],"type":"journal_article","doi":"10.1021/jacs.4c16975","oa_version":"None","citation":{"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>","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.","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>","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>.","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>.","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.","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."},"date_created":"2025-02-23T23:01:56Z","article_type":"original","article_processing_charge":"No","month":"02","volume":147,"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"}],"isi":1,"department":[{"_id":"PaSc"}],"status":"public","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","external_id":{"pmid":["39955787"],"isi":["001423628600001"]},"OA_type":"closed access","day":"16","date_updated":"2025-09-30T10:36:53Z","page":"6813-6824","author":[{"first_name":"Alons","full_name":"Lends, Alons","last_name":"Lends"},{"full_name":"Lamon, Gaelle","last_name":"Lamon","first_name":"Gaelle"},{"last_name":"Delcourte","full_name":"Delcourte, Loic","first_name":"Loic"},{"first_name":"Aude","full_name":"Sturny-Leclere, Aude","last_name":"Sturny-Leclere"},{"full_name":"Grélard, Axelle","last_name":"Grélard","first_name":"Axelle"},{"full_name":"Morvan, Estelle","last_name":"Morvan","first_name":"Estelle"},{"last_name":"Abdul-Shukkoor","full_name":"Abdul-Shukkoor, Muhammed Bilal","first_name":"Muhammed Bilal"},{"first_name":"Mélanie","last_name":"Berbon","full_name":"Berbon, Mélanie"},{"first_name":"Alicia","last_name":"Vallet","full_name":"Vallet, Alicia"},{"full_name":"Habenstein, Birgit","last_name":"Habenstein","first_name":"Birgit"},{"first_name":"Erick J.","last_name":"Dufourc","full_name":"Dufourc, Erick J."},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda"},{"last_name":"Aimanianda","full_name":"Aimanianda, Vishukumar","first_name":"Vishukumar"},{"first_name":"Antoine","full_name":"Loquet, Antoine","last_name":"Loquet"}],"_id":"19072","publisher":"American Chemical Society","quality_controlled":"1","publication_status":"published"},{"publisher":"Wiley","has_accepted_license":"1","ddc":["540"],"_id":"19555","author":[{"first_name":"Darja","id":"81dc668a-19fa-11f0-bf31-d56534059ef3","last_name":"Rohden","full_name":"Rohden, Darja"},{"first_name":"Giorgia","full_name":"Toscano, Giorgia","last_name":"Toscano"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda"},{"first_name":"Roman J.","full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker"}],"file_date_updated":"2025-08-05T12:59:24Z","oa":1,"PlanS_conform":"1","quality_controlled":"1","corr_author":"1","publication_status":"published","project":[{"grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"day":"25","OA_type":"hybrid","external_id":{"isi":["001479486400019"],"pmid":["40080421"]},"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_updated":"2025-09-30T11:35:05Z","citation":{"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).","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>.","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."},"acknowledged_ssus":[{"_id":"NMR"}],"OA_place":"publisher","file":[{"access_level":"open_access","date_created":"2025-08-05T12:59:24Z","creator":"dernst","relation":"main_file","file_id":"20136","success":1,"checksum":"e3788628644b5aac666cf079b05f8fa7","content_type":"application/pdf","date_updated":"2025-08-05T12:59:24Z","file_size":2840681,"file_name":"2025_ChemistryEur_Rohden.pdf"}],"oa_version":"Published Version","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"article_type":"original","date_created":"2025-04-13T22:01:19Z","department":[{"_id":"PaSc"}],"isi":1,"volume":31,"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"}],"month":"04","article_processing_charge":"Yes (in subscription journal)","status":"public","pmid":1,"publication_identifier":{"eissn":["1521-3765"],"issn":["0947-6539"]},"article_number":"e202500408","title":"Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy","intvolume":"        31","year":"2025","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.","issue":"24","type":"journal_article","language":[{"iso":"eng"}],"date_published":"2025-04-25T00:00:00Z","publication":"Chemistry - A European Journal","scopus_import":"1","doi":"10.1002/chem.202500408"},{"title":"Dataset for \"Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State\"","year":"2025","day":"31","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","type":"research_data","date_published":"2025-07-31T00:00:00Z","date_updated":"2026-06-10T08:33:41Z","doi":"10.15479/AT-ISTA-19696","citation":{"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>","short":"B. Tatman, (2025).","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.","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>.","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>.","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>","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>."},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"publisher":"Institute of Science and Technology Austria","file":[{"creator":"btatman","date_created":"2025-07-31T08:14:40Z","relation":"main_file","file_id":"20094","access_level":"open_access","content_type":"application/zip","file_name":"dataset.zip","file_size":557878455,"date_updated":"2025-07-31T08:14:40Z","success":1,"checksum":"4c2d29404e070bda7d5619f728ec555c"},{"success":1,"checksum":"6cbccd602be0ecb6ddb1f81fdfcadf92","content_type":"text/plain","date_updated":"2025-07-31T08:14:21Z","file_size":3514,"file_name":"readme.txt","access_level":"open_access","date_created":"2025-07-31T08:14:21Z","creator":"btatman","relation":"main_file","file_id":"20095"}],"contributor":[{"contributor_type":"project_leader","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","orcid":"0000-0002-9350-7606"},{"contributor_type":"researcher","first_name":"Vidhyalakshmi","last_name":"Sridharan"},{"contributor_type":"researcher","first_name":"Motilal","last_name":"Uttarkabat"},{"contributor_type":"researcher","first_name":"Christopher","last_name":"Jaroniec"},{"last_name":"Ernst","first_name":"Matthias","contributor_type":"researcher"},{"last_name":"Rovo","orcid":"0000-0001-8729-7326","id":"c316e53f-b965-11eb-b128-bb26acc59c00","first_name":"Petra","contributor_type":"researcher"}],"has_accepted_license":"1","_id":"19696","author":[{"first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman","full_name":"Tatman, Benjamin"}],"oa_version":"Published Version","tmp":{"image":"/images/cc_by_nc_sa.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"file_date_updated":"2025-07-31T08:14:40Z","oa":1,"date_created":"2025-05-14T10:46:07Z","corr_author":"1","department":[{"_id":"PaSc"}],"month":"07","article_processing_charge":"No","status":"public","related_material":{"record":[{"id":"20321","status":"public","relation":"research_data"}],"link":[{"url":"http.//doi.org/10.1021/jacs.5c09057","description":"Paper to which the dataset corresponds.","relation":"research_paper"}]}},{"project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"}],"title":"Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme","day":"03","year":"2025","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","type":"research_data","date_published":"2025-07-03T00:00:00Z","doi":"10.15479/AT-ISTA-19956","date_updated":"2026-06-10T08:20:38Z","publisher":"Institute of Science and Technology Austria","citation":{"ista":"Schanda P. 2025. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-19956\">10.15479/AT-ISTA-19956</a>.","ieee":"P. Schanda, “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Institute of Science and Technology Austria, 2025.","apa":"Schanda, P. (2025). Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-19956\">https://doi.org/10.15479/AT-ISTA-19956</a>","mla":"Schanda, Paul. <i>Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme</i>. Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19956\">10.15479/AT-ISTA-19956</a>.","chicago":"Schanda, Paul. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-19956\">https://doi.org/10.15479/AT-ISTA-19956</a>.","ama":"Schanda P. Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme. 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19956\">10.15479/AT-ISTA-19956</a>","short":"P. Schanda, (2025)."},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"author":[{"orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"_id":"19956","oa_version":"Published Version","contributor":[{"last_name":"Rohden","first_name":"Darja","contributor_type":"researcher"},{"contributor_type":"researcher","first_name":"Federico","last_name":"Napoli"},{"first_name":"Ben","contributor_type":"researcher","last_name":"Tatman"},{"contributor_type":"researcher","first_name":"Paul","last_name":"Schanda"}],"ddc":["572"],"has_accepted_license":"1","file":[{"success":1,"checksum":"a2ef61aa9fb5313c7d426913eb0482c0","file_name":"README","date_updated":"2025-07-03T10:30:14Z","file_size":1160,"content_type":"application/octet-stream","access_level":"open_access","relation":"main_file","creator":"pschanda","date_created":"2025-07-03T10:30:14Z","file_id":"19960"},{"file_id":"19961","relation":"main_file","creator":"pschanda","date_created":"2025-07-03T10:30:55Z","access_level":"open_access","file_name":"data_Arg_MASNMR_Rohden.zip","date_updated":"2025-07-03T10:30:55Z","file_size":128597184,"content_type":"application/zip","checksum":"8fb77b96d0fcc95c9903005652207a8c","success":1},{"access_level":"open_access","relation":"main_file","creator":"pschanda","date_created":"2025-08-14T07:06:58Z","file_id":"20172","success":1,"checksum":"a60cc16d20b089c4bef94040a99cfba5","date_updated":"2025-08-14T07:06:58Z","file_name":"20240903_ubi_DN_Argd1C13_2D_spectra.tar.xz","file_size":4766564,"content_type":"application/x-xz"}],"file_date_updated":"2025-08-14T07:06:58Z","oa":1,"tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png"},"date_created":"2025-07-03T04:21:37Z","department":[{"_id":"PaSc"}],"corr_author":"1","article_processing_charge":"No","month":"07","abstract":[{"text":"The specific introduction of 1H-13C or 1H-15N moieties into otherwise deuterated proteins holds great potential for high-resolution solution and magic-angle spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues play key roles for example at active sites of enzymes. Taking advantage of a chemically synthesized Arg with a 13C-1H2 group in an otherwise deuterated backbone, we demonstrate here the usefulness of proton-detected arginine MAS NMR approaches to probe arginine dynamics. In experiments on crystalline ubiquitin and the 134 kDa tetrameric enzyme malate dehydrogenase we detected a wide range of motions, from sites that are rigid on time scales of at least tens of milliseconds to residues undergoing predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled quantitative determination of these dynamics. We observed microsecond dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different β-turn conformations on this time scale. The labeling scheme and experiments presented here expand the toolkit for high-resolution proton-detected MAS NMR","lang":"eng"}],"status":"public","related_material":{"record":[{"status":"public","id":"20258","relation":"used_in_publication"}]}},{"date_created":"2025-08-17T22:01:35Z","article_type":"original","tmp":{"image":"/images/cc_by_nc_nd.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)"},"oa_version":"Published Version","OA_place":"publisher","citation":{"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>","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>.","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>.","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>","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."},"status":"public","article_processing_charge":"Yes","volume":8,"month":"08","abstract":[{"lang":"eng","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."}],"isi":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","year":"2025","intvolume":"         8","title":"The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa","pmid":1,"publication_identifier":{"eissn":["2399-3642"]},"article_number":"1148","doi":"10.1038/s42003-025-08589-5","scopus_import":"1","publication":"Communications Biology","date_published":"2025-08-02T00:00:00Z","language":[{"iso":"eng"}],"type":"journal_article","oa":1,"author":[{"last_name":"Castell","full_name":"Castell, Sofía D.","first_name":"Sofía D."},{"first_name":"Consuelo M.","last_name":"Fernandez","full_name":"Fernandez, Consuelo M."},{"first_name":"Ignacio N.","full_name":"Tumas, Ignacio N.","last_name":"Tumas"},{"first_name":"Lucía M.","last_name":"Margara","full_name":"Margara, Lucía M."},{"id":"273e0cbd-72f0-11ef-b75a-f9f932e292fa","first_name":"Maria C","last_name":"Miserendino","full_name":"Miserendino, Maria C"},{"last_name":"Ceschin","full_name":"Ceschin, Danilo G.","first_name":"Danilo G."},{"first_name":"Roberto J.","full_name":"Pezza, Roberto J.","last_name":"Pezza"},{"last_name":"Monti","full_name":"Monti, Mariela R.","first_name":"Mariela R."}],"_id":"20184","has_accepted_license":"1","ddc":["570"],"publisher":"Springer Nature","publication_status":"published","DOAJ_listed":"1","PlanS_conform":"1","quality_controlled":"1","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","day":"02","external_id":{"pmid":["40753298"],"isi":["001541878500001"]},"OA_type":"gold","date_updated":"2025-09-30T14:18:46Z","main_file_link":[{"url":"https://doi.org/10.1038/s42003-025-08589-5","open_access":"1"}]},{"has_accepted_license":"1","file":[{"checksum":"055044b03f835cb98c45d0504f1db96e","success":1,"file_size":42368943,"date_updated":"2025-08-31T15:09:44Z","file_name":"Abstracts.zip","content_type":"application/zip","access_level":"open_access","file_id":"20244","relation":"main_file","date_created":"2025-08-31T15:09:44Z","creator":"pschanda"},{"relation":"main_file","creator":"pschanda","date_created":"2025-08-31T15:11:58Z","file_id":"20245","access_level":"open_access","file_name":"data_CO2_conferences.zip","file_size":470659,"date_updated":"2025-08-31T15:11:58Z","content_type":"application/zip","success":1,"checksum":"1492683af736ac65088b77e12b52c3b0"},{"access_level":"open_access","file_id":"20246","date_created":"2025-08-31T15:12:03Z","creator":"pschanda","relation":"main_file","checksum":"8ac69071f7508e77b5ca91fa5018339a","success":1,"content_type":"application/zip","file_size":1138772,"date_updated":"2025-08-31T15:12:03Z","file_name":"Figure6_predictions.zip"},{"date_updated":"2025-08-31T15:12:07Z","file_size":6558,"file_name":"ExcelFileAnalysisCode.py","content_type":"text/x-python-script","checksum":"19b77db247feecdc36fbe6f68d94a76d","success":1,"file_id":"20247","relation":"main_file","creator":"pschanda","date_created":"2025-08-31T15:12:07Z","access_level":"open_access"},{"access_level":"open_access","file_id":"20248","relation":"main_file","date_created":"2025-08-31T15:12:11Z","creator":"pschanda","checksum":"39655e28c6df523f4f9662dc58c94623","success":1,"file_name":"emissions_spectrometers_and_Parisgoal.pdf","date_updated":"2025-08-31T15:12:11Z","file_size":1107467,"content_type":"application/pdf"},{"file_id":"20263","creator":"pschanda","date_created":"2025-09-01T11:05:27Z","relation":"main_file","access_level":"open_access","content_type":"application/octet-stream","file_size":3994,"file_name":"README","date_updated":"2025-09-01T11:05:27Z","checksum":"2e9a9460b3f2abe7e46179561a63492b","success":1}],"contributor":[{"last_name":"Ruzickova","contributor_type":"researcher","id":"D2761128-D73D-11E9-A1BF-BA0DE6697425","first_name":"Natalia"},{"contributor_type":"researcher","first_name":"Lucky","id":"84b9700b-15b2-11ec-abd3-831089e67615","last_name":"Kapoor"},{"last_name":"Leitner","id":"4c665ce3-0016-11ec-bea0-e44de7a4fa3d","first_name":"Valentin","contributor_type":"researcher"},{"id":"68AA0E5A-AFDA-11E9-9994-141DE6697425","first_name":"Predrag","contributor_type":"researcher","last_name":"Zivadinovic"},{"contributor_type":"researcher","first_name":"Maria A","id":"44A03D04-AEA4-11E9-B225-EA2DE6697425","last_name":"Sisak"},{"contributor_type":"researcher","id":"2a69ab4b-896a-11ed-bdf8-cb8641cf2b21","first_name":"Cecelia N","last_name":"Mweka"},{"last_name":"Dobbelaere","contributor_type":"supervisor","id":"c15a5412-de82-11ed-b809-8dc1aa996e40","first_name":"Jeroen A"},{"contributor_type":"supervisor","id":"38DB5788-F248-11E8-B48F-1D18A9856A87","first_name":"Georgios","orcid":"0000-0001-8342-202X","last_name":"Katsaros"}],"author":[{"first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"}],"_id":"20242","oa_version":"Published Version","citation":{"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>","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>.","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>.","ieee":"P. Schanda, “Data of: ‘Quantifying the carbon footprint of conference travel: the case of NMR meetings.’” Institute of Science and Technology Austria, 2025.","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>."},"publisher":"Institute of Science and Technology Austria","date_created":"2025-08-31T15:14:18Z","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png"},"file_date_updated":"2025-09-01T11:05:27Z","oa":1,"month":"09","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."}],"article_processing_charge":"No","corr_author":"1","department":[{"_id":"PaSc"}],"related_material":{"record":[{"status":"public","id":"20664","relation":"used_in_publication"}]},"status":"public","title":"Data of: \"Quantifying the carbon footprint of conference travel: the case of NMR meetings\"","keyword":["sustainability","conference travel"],"user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","year":"2025","date_published":"2025-09-01T00:00:00Z","type":"research_data","date_updated":"2026-06-10T08:45:12Z","doi":"10.15479/AT-ISTA-20242"},{"publisher":"Elsevier","has_accepted_license":"1","ddc":["540"],"author":[{"first_name":"Darja","id":"81dc668a-19fa-11f0-bf31-d56534059ef3","full_name":"Rohden, Darja","last_name":"Rohden"},{"orcid":"0000-0002-9043-136X","last_name":"Napoli","full_name":"Napoli, Federico","first_name":"Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b"},{"last_name":"Kapitonova","full_name":"Kapitonova, Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna"},{"full_name":"Tatman, Benjamin","last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin"},{"first_name":"Roman J.","full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker"},{"full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"_id":"20258","oa":1,"file_date_updated":"2025-12-29T14:51:40Z","PlanS_conform":"1","corr_author":"1","quality_controlled":"1","publication_status":"published","project":[{"grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery"}],"day":"01","OA_type":"hybrid","external_id":{"isi":["001618289100020"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2026-06-10T08:20:37Z","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"citation":{"ama":"Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>","short":"D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda, Journal of Molecular Biology 437 (2025).","ista":"Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. 2025. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. Journal of Molecular Biology. 437(23), 169379.","ieee":"D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R. J. Lichtenecker, and P. Schanda, “Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025.","apa":"Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &#38; Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>","mla":"Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169379, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>.","chicago":"Rohden, Darja, Federico Napoli, Anna Kapitonova, Benjamin Tatman, Roman J. Lichtenecker, and Paul Schanda. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>."},"OA_place":"publisher","file":[{"checksum":"90d50594d8ea9860ac5da41297992847","success":1,"content_type":"application/pdf","file_size":2270555,"file_name":"2025_JourMolecularBiology_Rohden.pdf","date_updated":"2025-12-29T14:51:40Z","access_level":"open_access","file_id":"20876","date_created":"2025-12-29T14:51:40Z","creator":"dernst","relation":"main_file"}],"oa_version":"Published Version","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"date_created":"2025-08-31T22:01:33Z","article_type":"original","department":[{"_id":"PaSc"}],"month":"12","volume":437,"abstract":[{"text":"The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise deuterated proteins holds great potential for high-resolution solution and magic-angle spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues play key roles for example at active sites of enzymes. Taking advantage of a chemically synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we demonstrate here the usefulness of proton-detected MAS NMR approaches to probe arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric enzyme malate dehydrogenase we detected a wide range of motions, from sites that are rigid on time scales of at least tens of milliseconds to residues undergoing predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled quantitative determination of these dynamics. We observed microsecond dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different β-turn conformations on this time scale. The labeling scheme and experiments presented here expand the toolkit for high-resolution proton-detected MAS NMR.","lang":"eng"}],"isi":1,"article_processing_charge":"Yes (via OA deal)","status":"public","related_material":{"record":[{"relation":"research_data","id":"19956","status":"public"}]},"article_number":"169379","publication_identifier":{"eissn":["1089-8638"],"issn":["0022-2836"]},"title":"Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme","intvolume":"       437","year":"2025","issue":"23","acknowledgement":"This work was supported financially by the Austrian Science Fund (FWF, Grant No. I5812-B, “AlloSpace”). 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 (LSF). We thank Petra Rovò and Margarita Valhondo Falcón for excellent support of the NMR facility.","type":"journal_article","language":[{"iso":"eng"}],"date_published":"2025-12-01T00:00:00Z","publication":"Journal of Molecular Biology","scopus_import":"1","doi":"10.1016/j.jmb.2025.169379"},{"title":"Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR","publication_identifier":{"eissn":["1520-5126"],"issn":["0002-7863"]},"pmid":1,"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.","issue":"32","intvolume":"       147","year":"2025","date_published":"2025-08-01T00:00:00Z","publication":"Journal of the American Chemical Society","language":[{"iso":"eng"}],"scopus_import":"1","type":"journal_article","doi":"10.1021/jacs.5c09057","file":[{"access_level":"open_access","relation":"main_file","creator":"dernst","date_created":"2025-09-10T07:53:10Z","file_id":"20337","success":1,"checksum":"b350d56ddddefea96cebd62c277c0ff5","file_name":"2025_JACS_Tatman.pdf","date_updated":"2025-09-10T07:53:10Z","file_size":5235353,"content_type":"application/pdf"}],"oa_version":"Published Version","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"citation":{"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>.","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>","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>.","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.","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.","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>","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."},"OA_place":"publisher","article_type":"original","date_created":"2025-09-10T05:37:19Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"volume":147,"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."}],"isi":1,"month":"08","article_processing_charge":"Yes (via OA deal)","department":[{"_id":"PaSc"},{"_id":"NMR"}],"related_material":{"record":[{"status":"public","id":"19696","relation":"used_in_publication"}]},"status":"public","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","external_id":{"isi":["001542746200001"],"pmid":["40748291"]},"OA_type":"hybrid","day":"01","date_updated":"2026-06-10T08:33:41Z","page":"29315-29326","ddc":["540"],"has_accepted_license":"1","_id":"20321","author":[{"first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin","last_name":"Tatman"},{"last_name":"Sridharan","full_name":"Sridharan, Vidhyalakshmi","first_name":"Vidhyalakshmi"},{"last_name":"Uttarkabat","full_name":"Uttarkabat, Motilal","first_name":"Motilal"},{"first_name":"Christopher P.","last_name":"Jaroniec","full_name":"Jaroniec, Christopher P."},{"first_name":"Matthias","last_name":"Ernst","full_name":"Ernst, Matthias"},{"first_name":"Petra","id":"c316e53f-b965-11eb-b128-bb26acc59c00","full_name":"Rovo, Petra","last_name":"Rovo","orcid":"0000-0001-8729-7326"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda"}],"publisher":"American Chemical Society","file_date_updated":"2025-09-10T07:53:10Z","oa":1,"corr_author":"1","quality_controlled":"1","PlanS_conform":"1","publication_status":"published"},{"status":"public","month":"12","volume":437,"abstract":[{"lang":"eng","text":"In this study, we describe an integrated approach for methyl group assignment comprising precursor-based selective methyl group labeling, a novel pulse sequence for methyl to backbone coherence transfer and chemical shift predictions using UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal methyl groups of leucine and valine residues to each other and to the protein backbone. By additional 13C,2H-labeling of residues other than valine and leucine residues of the protein, important chemical shift information about neighboring residues (following valine and leucine residues) can be achieved. Thus, different valine and leucine residues in a protein can be characterized as a specific chemical shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0 using experimental data taken from a subset of the BMRB database revealed a correct assignment performance of about 90%. With applications to proteins of 60.2 kDa and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides valuable information even for very large proteins."}],"article_processing_charge":"Yes (in subscription journal)","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"article_type":"original","date_created":"2025-10-26T23:01:35Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"file":[{"success":1,"checksum":"feb92f9c79032c261165f4ca573f444a","content_type":"application/pdf","date_updated":"2025-12-30T10:29:08Z","file_size":3076611,"file_name":"2025_JourMolecularBiology_Knoedlstorfer.pdf","access_level":"open_access","creator":"dernst","date_created":"2025-12-30T10:29:08Z","relation":"main_file","file_id":"20915"}],"oa_version":"Published Version","citation":{"short":"S. Knödlstorfer, G. Toscano, A.L. Ptaszek, G. Kontaxis, F. Napoli, J. Schneider, K. Maier, A. Kapitonova, R.J. Lichtenecker, P. Schanda, R. Konrat, Journal of Molecular Biology 437 (2025).","ama":"Knödlstorfer S, Toscano G, Ptaszek AL, et al. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>","ieee":"S. Knödlstorfer <i>et al.</i>, “A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025.","ista":"Knödlstorfer S, Toscano G, Ptaszek AL, Kontaxis G, Napoli F, Schneider J, Maier K, Kapitonova A, Lichtenecker RJ, Schanda P, Konrat R. 2025. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal of Molecular Biology. 437(23), 169465.","chicago":"Knödlstorfer, Sonja, Giorgia Toscano, Aleksandra L. Ptaszek, Georg Kontaxis, Federico Napoli, Jakob Schneider, Katharina Maier, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>.","apa":"Knödlstorfer, S., Toscano, G., Ptaszek, A. L., Kontaxis, G., Napoli, F., Schneider, J., … Konrat, R. (2025). A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>","mla":"Knödlstorfer, Sonja, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169465, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>."},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"OA_place":"publisher","doi":"10.1016/j.jmb.2025.169465","language":[{"iso":"eng"}],"date_published":"2025-12-01T00:00:00Z","publication":"Journal of Molecular Biology","scopus_import":"1","type":"journal_article","acknowledgement":"A.L.P and G.T were funded by the “New Ideas” program by Vienna Doctoral School in Chemistry. S.K. was funded by the Austrian Science Fund FWF P35098-B. This work was supported financially by the Austrian Science Fund (FWF, grant numbers I06223 and I5812-B, “AlloSpace”). 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 (LSF). We thank Celina Sailer for assistance with the analysis of the NMR spectrum of HsTom70.","issue":"23","intvolume":"       437","year":"2025","title":"A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0","pmid":1,"article_number":"169465","publication_identifier":{"issn":["0022-2836"],"eissn":["1089-8638"]},"publication_status":"published","quality_controlled":"1","PlanS_conform":"1","oa":1,"file_date_updated":"2025-12-30T10:29:08Z","has_accepted_license":"1","ddc":["540"],"author":[{"full_name":"Knödlstorfer, Sonja","last_name":"Knödlstorfer","first_name":"Sonja"},{"id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","first_name":"Giorgia","full_name":"Toscano, Giorgia","last_name":"Toscano"},{"first_name":"Aleksandra L.","last_name":"Ptaszek","full_name":"Ptaszek, Aleksandra L."},{"first_name":"Georg","full_name":"Kontaxis, Georg","last_name":"Kontaxis"},{"orcid":"0000-0002-9043-136X","last_name":"Napoli","full_name":"Napoli, Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","first_name":"Federico"},{"last_name":"Schneider","full_name":"Schneider, Jakob","id":"64368429-eb97-11eb-a6c2-c980b1f44415","first_name":"Jakob"},{"last_name":"Maier","full_name":"Maier, Katharina","first_name":"Katharina"},{"last_name":"Kapitonova","full_name":"Kapitonova, Anna","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471"},{"first_name":"Roman J.","last_name":"Lichtenecker","full_name":"Lichtenecker, Roman J."},{"full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"full_name":"Konrat, Robert","last_name":"Konrat","first_name":"Robert"}],"_id":"20538","publisher":"Elsevier","date_updated":"2025-12-30T10:29:20Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"01","OA_type":"hybrid","external_id":{"pmid":["41016549"]},"project":[{"grant_number":"I06223","name":"Structure and mechanism of the mitochondrial MIM insertase","_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0"},{"grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery"}]},{"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"}],"month":"11","volume":6,"article_processing_charge":"Yes","department":[{"_id":"JoFi"},{"_id":"GaTk"},{"_id":"JoCs"},{"_id":"EvBe"},{"_id":"TaHa"},{"_id":"GradSch"},{"_id":"GeKa"},{"_id":"PaSc"}],"related_material":{"record":[{"relation":"research_data","status":"public","id":"20242"}],"link":[{"relation":"research_data","url":"https://ista.ac.at/en/news/carbon-footprint-of-conference-travel/","description":"News on ISTA website"}]},"status":"public","file":[{"content_type":"application/pdf","file_name":"2025_MagneticResonance_Kapoor.pdf","file_size":3081399,"date_updated":"2025-11-24T08:25:19Z","checksum":"c63dd47b0e77f9451821436bb77d27c9","success":1,"file_id":"20672","date_created":"2025-11-24T08:25:19Z","creator":"dernst","relation":"main_file","access_level":"open_access"}],"oa_version":"Published Version","citation":{"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.","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.","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>.","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>","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>.","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>","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."},"OA_place":"publisher","article_type":"original","date_created":"2025-11-23T23:01:39Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"language":[{"iso":"eng"}],"date_published":"2025-11-10T00:00:00Z","publication":"Magnetic Resonance","scopus_import":"1","type":"journal_article","doi":"10.5194/mr-6-243-2025","title":"Quantifying the carbon footprint of conference travel: The case of NMR meetings","publication_identifier":{"eissn":["2699-0016"]},"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).","issue":"2","intvolume":"         6","year":"2025","PlanS_conform":"1","corr_author":"1","quality_controlled":"1","DOAJ_listed":"1","publication_status":"published","has_accepted_license":"1","ddc":["000"],"_id":"20664","author":[{"first_name":"Lucky","id":"84b9700b-15b2-11ec-abd3-831089e67615","orcid":"0000-0001-8319-2148","last_name":"Kapoor","full_name":"Kapoor, Lucky"},{"first_name":"Natalia","id":"D2761128-D73D-11E9-A1BF-BA0DE6697425","last_name":"Ruzickova","full_name":"Ruzickova, Natalia"},{"last_name":"Zivadinovic","full_name":"Zivadinovic, Predrag","first_name":"Predrag","id":"68AA0E5A-AFDA-11E9-9994-141DE6697425"},{"full_name":"Leitner, Valentin","last_name":"Leitner","id":"4c665ce3-0016-11ec-bea0-e44de7a4fa3d","first_name":"Valentin"},{"first_name":"Maria A","id":"44A03D04-AEA4-11E9-B225-EA2DE6697425","last_name":"Sisak","full_name":"Sisak, Maria A"},{"full_name":"Mweka, Cecelia N","last_name":"Mweka","id":"2a69ab4b-896a-11ed-bdf8-cb8641cf2b21","first_name":"Cecelia N"},{"id":"c15a5412-de82-11ed-b809-8dc1aa996e40","first_name":"Jeroen A","full_name":"Dobbelaere, Jeroen A","last_name":"Dobbelaere"},{"full_name":"Katsaros, Georgios","last_name":"Katsaros","orcid":"0000-0001-8342-202X","id":"38DB5788-F248-11E8-B48F-1D18A9856A87","first_name":"Georgios"},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"publisher":"Copernicus Publications","APC_amount":"1260 EUR","oa":1,"file_date_updated":"2025-11-24T08:25:19Z","date_updated":"2026-06-10T08:45:11Z","page":"243-256","project":[{"_id":"B67AFEDC-15C9-11EA-A837-991A96BB2854","name":"IST Austria Open Access Fund"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"10","OA_type":"gold"},{"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"abstract":[{"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. ","lang":"eng"}],"month":"11","article_processing_charge":"No","status":"public","related_material":{"record":[{"id":"21145","status":"public","relation":"later_version"},{"relation":"used_in_publication","status":"public","id":"22105"}]},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"citation":{"short":"L.M. Becker, P. Schanda, (2025).","ama":"Becker LM, Schanda P. Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20641\">10.15479/AT-ISTA-20641</a>","chicago":"Becker, Lea Marie, and Paul Schanda. “Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-20641\">https://doi.org/10.15479/AT-ISTA-20641</a>.","apa":"Becker, L. M., &#38; Schanda, P. (2025). 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-20641\">https://doi.org/10.15479/AT-ISTA-20641</a>","mla":"Becker, Lea Marie, and Paul Schanda. <i>Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.”</i> Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20641\">10.15479/AT-ISTA-20641</a>.","ieee":"L. M. Becker and P. Schanda, “Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2025.","ista":"Becker LM, Schanda P. 2025. 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-20641\">10.15479/AT-ISTA-20641</a>."},"file":[{"checksum":"a73a0550c644957e7f62241e239d3a1d","date_updated":"2026-02-17T10:16:57Z","file_name":"Research_Data.zip","file_size":1806589513,"content_type":"application/zip","access_level":"open_access","relation":"main_file","creator":"lbecker","date_created":"2025-11-13T09:38:35Z","file_id":"20643"},{"file_id":"20652","relation":"table_of_contents","date_created":"2025-11-17T11:54:17Z","creator":"lbecker","access_level":"open_access","date_updated":"2026-02-17T10:16:57Z","file_name":"README.pdf","file_size":191376,"content_type":"application/pdf","checksum":"7176b257f753c213a0460ee06f802363"}],"oa_version":"Published Version","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png"},"date_created":"2025-11-13T09:29:58Z","type":"research_data","date_published":"2025-11-18T00:00:00Z","doi":"10.15479/AT-ISTA-20641","title":"Data for \"Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes\"","year":"2025","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.","corr_author":"1","publisher":"Institute of Science and Technology Austria","ddc":["572"],"has_accepted_license":"1","contributor":[{"last_name":"Fu","contributor_type":"researcher","first_name":"Haohao "},{"contributor_type":"researcher","first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman"},{"last_name":"Dreydoppel","contributor_type":"researcher","first_name":"Matthias"},{"contributor_type":"researcher","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","last_name":"Kapitonova"},{"id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","first_name":"Daniel","contributor_type":"researcher","orcid":"0000-0001-7597-043X","last_name":"Balazs"},{"last_name":"Weininger","contributor_type":"researcher","first_name":"Ulrich"},{"first_name":"Sylvain","contributor_type":"researcher","last_name":"Engilberge"},{"contributor_type":"researcher","first_name":"Christophe","last_name":"Chipot"}],"author":[{"first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151"},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"_id":"20641","file_date_updated":"2026-02-17T10:16:57Z","oa":1,"date_updated":"2026-06-24T08:47:57Z","project":[{"grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0"}],"day":"18","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d"},{"pmid":1,"publication_identifier":{"issn":["2699-0016"]},"title":"Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck","intvolume":"         5","year":"2024","acknowledgement":"We thank Dominique Madern (IBS Grenoble) for providing the plasmid for MalDH and feedback on the article, Alicia Vallet for excellent support at the Grenoble NMR facility, and Petra Rovo and Margarita Valhondo at the IST Austria NMR Service Unit. We thank Dorothea Anrather in the mass spectrometry facility of Max Perutz Labs for the mass spectrometry analysis using the instruments of the Vienna BioCenter Core Facilities (VBCF). We are grateful to Jean-Pierre Andrieu (Plateforme Seq3A, IBS Grenoble) for the analysis of the amino acid composition of the in-house-prepared lysates. We are grateful to Rasmus Linser (Technical University Dortmund) for sharing a paper draft describing a similar study. This work was supported by the Austrian Science Fund (FWF; project number I5812-B). We thank Tobias Schubeis (Lyon) and the reviewers for constructive input.\r\nThis research has been supported by the Austrian Science Fund (grant no. I5812-B). Part of this work used the platforms of the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for 40 Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). IBS acknowledges integration into the Interdisciplinary Research Institute of Grenoble (IRIG, 45 CEA). Charles-Adrien Arnaud was funded by GRAL.","issue":"1","type":"journal_article","date_published":"2024-04-19T00:00:00Z","publication":"Magnetic Resonance","language":[{"iso":"eng"}],"scopus_import":"1","doi":"10.5194/mr-5-33-2024","acknowledged_ssus":[{"_id":"NMR"}],"citation":{"short":"F. Napoli, J.-Y. Guan, C.-A. Arnaud, P. Macek, H. Fraga, C. Breyton, P. Schanda, Magnetic Resonance 5 (2024) 33–49.","ama":"Napoli F, Guan J-Y, Arnaud C-A, et al. Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. <i>Magnetic Resonance</i>. 2024;5(1):33-49. doi:<a href=\"https://doi.org/10.5194/mr-5-33-2024\">10.5194/mr-5-33-2024</a>","chicago":"Napoli, Federico, Jia-Ying Guan, Charles-Adrien Arnaud, Pavel Macek, Hugo Fraga, Cécile Breyton, and Paul Schanda. “Deuteration of Proteins Boosted by Cell Lysates: High-Resolution Amide and Ha Magic-Angle-Spinning (MAS) NMR without the Reprotonation Bottleneck.” <i>Magnetic Resonance</i>. Copernicus Publications, 2024. <a href=\"https://doi.org/10.5194/mr-5-33-2024\">https://doi.org/10.5194/mr-5-33-2024</a>.","apa":"Napoli, F., Guan, J.-Y., Arnaud, C.-A., Macek, P., Fraga, H., Breyton, C., &#38; Schanda, P. (2024). Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-5-33-2024\">https://doi.org/10.5194/mr-5-33-2024</a>","mla":"Napoli, Federico, et al. “Deuteration of Proteins Boosted by Cell Lysates: High-Resolution Amide and Ha Magic-Angle-Spinning (MAS) NMR without the Reprotonation Bottleneck.” <i>Magnetic Resonance</i>, vol. 5, no. 1, Copernicus Publications, 2024, pp. 33–49, doi:<a href=\"https://doi.org/10.5194/mr-5-33-2024\">10.5194/mr-5-33-2024</a>.","ista":"Napoli F, Guan J-Y, Arnaud C-A, Macek P, Fraga H, Breyton C, Schanda P. 2024. Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. Magnetic Resonance. 5(1), 33–49.","ieee":"F. Napoli <i>et al.</i>, “Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck,” <i>Magnetic Resonance</i>, vol. 5, no. 1. Copernicus Publications, pp. 33–49, 2024."},"OA_place":"publisher","file":[{"date_updated":"2024-05-22T07:01:15Z","file_name":"2024_MagneticResonance_Napoli.pdf","file_size":6657865,"content_type":"application/pdf","checksum":"80ea50114e428461ca9530d3bd5d89e4","success":1,"file_id":"15413","relation":"main_file","creator":"dernst","date_created":"2024-05-22T07:01:15Z","access_level":"open_access"}],"oa_version":"Published Version","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"date_created":"2024-05-16T15:02:43Z","article_type":"original","department":[{"_id":"PaSc"}],"abstract":[{"text":"Amide-proton-detected magic-angle-spinning NMR of deuterated proteins has become a main technique in NMR-based structural biology. In standard deuteration protocols that rely on D2O-based culture media, non-exchangeable amide sites remain deuterated, making these sites unobservable. Here we demonstrate that proteins produced with a H2O-based culture medium doped with deuterated cell lysate allow scientists to overcome this “reprotonation bottleneck” while retaining a high level of deuteration (ca. 80 %) and narrow linewidths. We quantified coherence lifetimes of several proteins prepared with this labeling pattern over a range of magic-angle-spinning (MAS) frequencies (40–100 kHz). We demonstrate that under commonly used conditions (50–60 kHz MAS), the amide 1H linewidths with our labeling approach are comparable to those of perdeuterated proteins and better than those of protonated samples at 100 kHz. For three proteins in the 33–50 kDa size range, many previously unobserved amides become visible. We report how to prepare the deuterated cell lysate for our approach from fractions of perdeuterated cultures which are usually discarded, and we show that such media can be used identically to commercial media. The residual protonation of Hα sites allows for well-resolved Hα-detected spectra and Hα resonance assignment, exemplified by the de novo assignment of 168 Hα sites in a 39 kDa protein. The approach based on this H2O/cell-lysate deuteration and MAS frequencies compatible with 1.3 or 1.9 mm rotors presents a strong sensitivity benefit over 0.7 mm 100 kHz MAS experiments.","lang":"eng"}],"month":"04","volume":5,"article_processing_charge":"Yes","status":"public","project":[{"name":"AlloSpace. The emergence and mechanisms of allostery","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812"},{"name":"FWF Open Access Fund","_id":"3AC91DDA-15DF-11EA-824D-93A3E7B544D1","call_identifier":"FWF"}],"external_id":{"pmid":["40384771"]},"OA_type":"gold","day":"19","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"33-49","date_updated":"2025-07-17T08:12:23Z","publisher":"Copernicus Publications","has_accepted_license":"1","ddc":["530"],"author":[{"first_name":"Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","orcid":"0000-0002-9043-136X","last_name":"Napoli","full_name":"Napoli, Federico"},{"last_name":"Guan","full_name":"Guan, Jia-Ying","first_name":"Jia-Ying"},{"first_name":"Charles-Adrien","last_name":"Arnaud","full_name":"Arnaud, Charles-Adrien"},{"last_name":"Macek","full_name":"Macek, Pavel","first_name":"Pavel"},{"first_name":"Hugo","full_name":"Fraga, Hugo","last_name":"Fraga"},{"last_name":"Breyton","full_name":"Breyton, Cécile","first_name":"Cécile"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul"}],"_id":"15401","APC_amount":"1530 EUR","file_date_updated":"2024-05-22T07:01:15Z","oa":1,"corr_author":"1","quality_controlled":"1","publication_status":"published"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2024","day":"22","title":"Raw data to \"MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments\"","keyword":["nuclear magnetic resonance","NMR","cellwall","structural biology","spectroscopy"],"date_updated":"2025-09-09T12:01:41Z","doi":"10.15479/AT:ISTA:17042","date_published":"2024-05-22T00:00:00Z","type":"research_data","date_created":"2024-05-22T12:04:54Z","tmp":{"image":"/images/cc_by_nc_nd.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)"},"file_date_updated":"2024-05-22T12:17:10Z","oa":1,"contributor":[{"last_name":"Vallet","first_name":"Alicia","contributor_type":"data_collector"},{"contributor_type":"data_collector","first_name":"Isabel ","last_name":"Ayala"},{"last_name":"Perrone","first_name":"Barbara","contributor_type":"data_collector"},{"last_name":"Hassan","contributor_type":"data_collector","first_name":"Alia"},{"last_name":"Bougault","first_name":"Catherine","contributor_type":"data_collector"}],"ddc":["570"],"file":[{"date_created":"2024-05-22T12:05:13Z","creator":"pschanda","relation":"main_file","file_id":"17043","access_level":"open_access","content_type":"text/plain","file_name":"Read_me.txt","file_size":2132,"date_updated":"2024-05-22T12:05:13Z","success":1,"checksum":"eb55f0988342d927702353b75e07edfa"},{"access_level":"open_access","creator":"pschanda","date_created":"2024-05-22T12:17:10Z","relation":"main_file","file_id":"17044","success":1,"checksum":"3393592acaf5ee1e032052c236780914","content_type":"application/zip","file_size":755704888,"date_updated":"2024-05-22T12:17:10Z","file_name":"raw_data_CryoMAS_cyronebacteria.zip"}],"has_accepted_license":"1","_id":"17042","oa_version":"Published Version","author":[{"first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606"}],"citation":{"ieee":"P. Schanda, “Raw data to ‘MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.’” Institute of Science and Technology Austria, 2024.","ista":"Schanda P. 2024. Raw data to ‘MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT:ISTA:17042\">10.15479/AT:ISTA:17042</a>.","chicago":"Schanda, Paul. “Raw Data to ‘MAS NMR Experiments of Corynebacterial Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.’” Institute of Science and Technology Austria, 2024. <a href=\"https://doi.org/10.15479/AT:ISTA:17042\">https://doi.org/10.15479/AT:ISTA:17042</a>.","apa":"Schanda, P. (2024). Raw data to “MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:17042\">https://doi.org/10.15479/AT:ISTA:17042</a>","mla":"Schanda, Paul. <i>Raw Data to “MAS NMR Experiments of Corynebacterial Cell Walls: Complementary 1H- and CPMAS CryoProbe-Enhanced 13C-Detected Experiments.”</i> Institute of Science and Technology Austria, 2024, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:17042\">10.15479/AT:ISTA:17042</a>.","short":"P. Schanda, (2024).","ama":"Schanda P. Raw data to “MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.” 2024. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:17042\">10.15479/AT:ISTA:17042</a>"},"publisher":"Institute of Science and Technology Austria","related_material":{"record":[{"relation":"used_in_publication","id":"17291","status":"public"}]},"status":"public","month":"05","abstract":[{"lang":"eng","text":"Bacterial cell walls are gigadalton-large cross-linked polymers with a wide range of motional amplitudes, including rather rigid as well as highly flexible parts. Magic-angle spinning NMR is a powerful method to obtain atomic-level information about intact cell walls. Here we investigate sensitivity and information content of different homonuclear 13C-13C and heteronuclear H-N, H-C and N-C correlation experiments. We demonstrate that a CPMAS CryoProbe yields ca. 8-fold increased signal-to-noise over a room-temperature probe, or a ca. 3-4-fold larger per-mass sensitivity. The increased sensitivity allowed to obtain high-resolution spectra even on intact bacteria. Moreover, we compare resolution and sensitivity of 1H MAS experiments obtained at 100 kHz vs. 55 kHz. Our study provides useful hints for choosing experiments to extract atomic-level details on cell-wall samples. "}],"article_processing_charge":"No","corr_author":"1","department":[{"_id":"PaSc"}]},{"issue":"1","acknowledgement":"We would like to thank Kay Saalwächter for pointing out important aspects of the intermediate regime during the open review process. Lea Marie Becker is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria.\r\nThis research has been supported by the Österreichischen Akademie der Wissenschaften (grant no. PR10660EAW01) and the Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (grant nos. 200020_188988 and 200020_219375).","year":"2024","intvolume":"         5","title":"Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR","pmid":1,"publication_identifier":{"eissn":["2699-0016"]},"doi":"10.5194/mr-5-69-2024","scopus_import":"1","date_published":"2024-06-11T00:00:00Z","publication":"Magnetic Resonance","language":[{"iso":"eng"}],"type":"journal_article","article_type":"original","date_created":"2024-06-23T22:01:02Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"oa_version":"Published Version","file":[{"access_level":"open_access","date_created":"2024-06-27T06:42:55Z","creator":"dernst","relation":"main_file","file_id":"17181","success":1,"checksum":"d01074f6919387fcaf8c9ebed320ccae","content_type":"application/pdf","date_updated":"2024-06-27T06:42:55Z","file_size":6736194,"file_name":"2024_MagneticResonance_Aebischer.pdf"}],"citation":{"chicago":"Aebischer, Kathrin, Lea Marie Becker, Paul Schanda, and Matthias Ernst. “Evaluating the Motional Timescales Contributing to Averaged Anisotropic Interactions in MAS Solid-State NMR.” <i>Magnetic Resonance</i>. Copernicus Publications, 2024. <a href=\"https://doi.org/10.5194/mr-5-69-2024\">https://doi.org/10.5194/mr-5-69-2024</a>.","apa":"Aebischer, K., Becker, L. M., Schanda, P., &#38; Ernst, M. (2024). Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-5-69-2024\">https://doi.org/10.5194/mr-5-69-2024</a>","mla":"Aebischer, Kathrin, et al. “Evaluating the Motional Timescales Contributing to Averaged Anisotropic Interactions in MAS Solid-State NMR.” <i>Magnetic Resonance</i>, vol. 5, no. 1, Copernicus Publications, 2024, pp. 69–86, doi:<a href=\"https://doi.org/10.5194/mr-5-69-2024\">10.5194/mr-5-69-2024</a>.","ieee":"K. Aebischer, L. M. Becker, P. Schanda, and M. Ernst, “Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR,” <i>Magnetic Resonance</i>, vol. 5, no. 1. Copernicus Publications, pp. 69–86, 2024.","ista":"Aebischer K, Becker LM, Schanda P, Ernst M. 2024. Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. Magnetic Resonance. 5(1), 69–86.","short":"K. Aebischer, L.M. Becker, P. Schanda, M. Ernst, Magnetic Resonance 5 (2024) 69–86.","ama":"Aebischer K, Becker LM, Schanda P, Ernst M. Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. <i>Magnetic Resonance</i>. 2024;5(1):69-86. doi:<a href=\"https://doi.org/10.5194/mr-5-69-2024\">10.5194/mr-5-69-2024</a>"},"status":"public","article_processing_charge":"Yes","abstract":[{"text":"Dynamic processes in molecules can occur on a wide range of timescales, and it is important to understand which timescales of motion contribute to different parameters used in dynamics measurements. For spin relaxation, this can easily be understood from the sampling frequencies of the spectral-density function by different relaxation-rate constants. In addition to data from relaxation measurements, determining dynamically averaged anisotropic interactions in magic-angle spinning (MAS) solid-state NMR allows for better quantification of the amplitude of molecular motion. For partially averaged anisotropic interactions, the relevant timescales of motion are not so clearly defined. Whether the averaging depends on the experimental methods (e.g., pulse sequences) or conditions (e.g., MAS frequency, magnitude of anisotropic interaction, radio-frequency field amplitudes) is not fully understood. To investigate these questions, we performed numerical simulations of dynamic systems based on the stochastic Liouville equation using several experiments for recoupling the dipolar coupling, chemical-shift anisotropy or quadrupolar coupling. As described in the literature, the transition between slow motion, where parameters characterizing the anisotropic interaction are not averaged, and fast motion, where the tensors are averaged leading to a scaled anisotropic quantity, occurs over a window of motional rate constants that depends mainly on the strength of the interaction. This transition region can span 2 orders of magnitude in exchange-rate constants (typically in the microsecond range) but depends only marginally on the employed recoupling scheme or sample spinning frequency. The transition region often coincides with a fast relaxation of coherences, making precise quantitative measurements difficult. Residual couplings in off-magic-angle experiments, however, average over longer timescales of motion. While in principle one may gain information on the timescales of motion from the transition area, extracting such information is hampered by low signal-to-noise ratio in experimental spectra due to fast relaxation that occurs in the same region.","lang":"eng"}],"month":"06","volume":5,"department":[{"_id":"PaSc"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["40384772"]},"day":"11","project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777"}],"date_updated":"2025-06-11T13:26:12Z","page":"69-86","file_date_updated":"2024-06-27T06:42:55Z","oa":1,"author":[{"full_name":"Aebischer, Kathrin","last_name":"Aebischer","first_name":"Kathrin"},{"orcid":"0000-0002-6401-5151","last_name":"Becker","full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie"},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Matthias","full_name":"Ernst, Matthias","last_name":"Ernst"}],"_id":"17161","has_accepted_license":"1","ddc":["530"],"publisher":"Copernicus Publications","publication_status":"published","quality_controlled":"1"}]