--- OA_place: repository OA_type: free access _id: '21284' 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. acknowledged_ssus: - _id: NMR - _id: LifeSc 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. article_processing_charge: No author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Becker LM, Schanda P. Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” 2026. doi:10.15479/AT-ISTA-21284 apa: Becker, L. M., & Schanda, P. (2026). Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-21284 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. https://doi.org/10.15479/AT-ISTA-21284. 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. 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, 10.15479/AT-ISTA-21284. mla: 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, doi:10.15479/AT-ISTA-21284. short: L.M. Becker, P. Schanda, (2026). contributor: - contributor_type: researcher first_name: Giorgia id: 334a5e40-8747-11f0-b671-ba1f5154b4b4 last_name: Toscano - contributor_type: researcher first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: researcher first_name: Rajkumar id: a3089acd-6806-11ee-bacc-f0c7d500ad20 last_name: Singh - contributor_type: researcher first_name: Undina id: bb74f472-ae54-11eb-9835-bc9c22fb1183 last_name: Guillerm - contributor_type: researcher first_name: Roman last_name: Lichtenecker corr_author: '1' date_created: 2026-02-17T10:17:14Z date_published: 2026-02-18T00:00:00Z date_updated: 2026-06-10T09:28:41Z day: '18' ddc: - '541' department: - _id: GradSch - _id: PaSc doi: 10.15479/AT-ISTA-21284 file: - access_level: open_access checksum: 2d3105f26be578073b88ee1f2ea0bdb1 content_type: application/zip creator: lbecker date_created: 2026-02-17T10:11:14Z date_updated: 2026-02-17T10:11:14Z file_id: '21285' file_name: Research_data.zip file_size: 36996027 relation: main_file success: 1 - access_level: open_access checksum: e24aebcdb8856cb181cbaa02de020ddb content_type: text/plain creator: lbecker date_created: 2026-02-17T10:11:14Z date_updated: 2026-02-17T10:11:14Z file_id: '21286' file_name: README.txt file_size: 1993 relation: table_of_contents file_date_updated: 2026-02-17T10:11:14Z has_accepted_license: '1' license: https://creativecommons.org/licenses/by-nc/4.0/ month: '2' oa: 1 oa_version: Published Version publisher: Institute of Science and Technology Austria status: public title: Research data for "Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants" tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2026' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '21929' abstract: - lang: eng 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.' 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. article_number: e70630 article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Jakob full_name: Schneider, Jakob id: 64368429-eb97-11eb-a6c2-c980b1f44415 last_name: Schneider - first_name: Undina full_name: Guillerm, Undina id: bb74f472-ae54-11eb-9835-bc9c22fb1183 last_name: Guillerm - first_name: Caroline full_name: Simoes Pereira, Caroline id: 87266c4a-96d2-11ef-be2c-fe5633233ec3 last_name: Simoes Pereira - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Schneider J, Guillerm U, Simoes Pereira C, Schanda P. Dynamic disorder is crucial for mitochondrial protein import. Protein Science. 2026;35(6). doi:10.1002/pro.70630 apa: Schneider, J., Guillerm, U., Simoes Pereira, C., & Schanda, P. (2026). Dynamic disorder is crucial for mitochondrial protein import. Protein Science. Wiley. https://doi.org/10.1002/pro.70630 chicago: Schneider, Jakob, Undina Guillerm, Caroline Simoes Pereira, and Paul Schanda. “Dynamic Disorder Is Crucial for Mitochondrial Protein Import.” Protein Science. Wiley, 2026. https://doi.org/10.1002/pro.70630. ieee: J. Schneider, U. Guillerm, C. Simoes Pereira, and P. Schanda, “Dynamic disorder is crucial for mitochondrial protein import,” Protein Science, vol. 35, no. 6. Wiley, 2026. ista: Schneider J, Guillerm U, Simoes Pereira C, Schanda P. 2026. Dynamic disorder is crucial for mitochondrial protein import. Protein Science. 35(6), e70630. mla: Schneider, Jakob, et al. “Dynamic Disorder Is Crucial for Mitochondrial Protein Import.” Protein Science, vol. 35, no. 6, e70630, Wiley, 2026, doi:10.1002/pro.70630. short: J. Schneider, U. Guillerm, C. Simoes Pereira, P. Schanda, Protein Science 35 (2026). corr_author: '1' date_created: 2026-05-31T22:02:12Z date_published: 2026-06-01T00:00:00Z date_updated: 2026-06-02T07:26:34Z day: '01' ddc: - '572' department: - _id: GradSch - _id: PaSc doi: 10.1002/pro.70630 external_id: pmid: - '42159315' file: - access_level: open_access checksum: e0163459a7238fdcc3fc5e17bedcce9a content_type: application/pdf creator: dernst date_created: 2026-06-02T07:23:12Z date_updated: 2026-06-02T07:23:12Z file_id: '21937' file_name: 2026_ProteinScience_Schneider.pdf file_size: 3897305 relation: main_file success: 1 file_date_updated: 2026-06-02T07:23:12Z has_accepted_license: '1' intvolume: ' 35' issue: '6' language: - iso: eng month: '06' oa: 1 oa_version: Published Version pmid: 1 project: - _id: bdb9578d-d553-11ed-ba76-ed5d39fce6f0 grant_number: I06223 name: Structure and mechanism of the mitochondrial MIM insertase publication: Protein Science publication_identifier: eissn: - 1469-896X issn: - 0961-8368 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: Dynamic disorder is crucial for mitochondrial protein import tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 35 year: '2026' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '21777' 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. acknowledged_ssus: - _id: NMR - _id: LifeSc 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). article_processing_charge: Yes article_type: original author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Giorgia full_name: Toscano, Giorgia id: 334a5e40-8747-11f0-b671-ba1f5154b4b4 last_name: Toscano - first_name: Anna full_name: Kapitonova, Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - first_name: Rajkumar full_name: Singh, Rajkumar id: a3089acd-6806-11ee-bacc-f0c7d500ad20 last_name: Singh - first_name: Undina full_name: Guillerm, Undina id: bb74f472-ae54-11eb-9835-bc9c22fb1183 last_name: Guillerm - first_name: Roman J. full_name: Lichtenecker, Roman J. last_name: Lichtenecker - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Becker LM, Toscano G, Kapitonova A, et al. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. Magnetic Resonance. 2026;7(1):29-37. doi:10.5194/mr-7-29-2026 apa: Becker, L. M., Toscano, G., Kapitonova, A., Singh, R., Guillerm, U., Lichtenecker, R. J., & Schanda, P. (2026). Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. Magnetic Resonance. Copernicus Publications. https://doi.org/10.5194/mr-7-29-2026 chicago: Becker, Lea Marie, Giorgia Toscano, Anna Kapitonova, Rajkumar Singh, Undina Guillerm, Roman J. Lichtenecker, and Paul Schanda. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” Magnetic Resonance. Copernicus Publications, 2026. https://doi.org/10.5194/mr-7-29-2026. ieee: L. M. Becker et al., “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants,” Magnetic Resonance, vol. 7, no. 1. Copernicus Publications, pp. 29–37, 2026. 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. mla: Becker, Lea Marie, et al. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” Magnetic Resonance, vol. 7, no. 1, Copernicus Publications, 2026, pp. 29–37, doi:10.5194/mr-7-29-2026. short: L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker, P. Schanda, Magnetic Resonance 7 (2026) 29–37. corr_author: '1' date_created: 2026-05-03T22:01:36Z date_published: 2026-04-16T00:00:00Z date_updated: 2026-07-20T09:49:12Z day: '16' ddc: - '540' department: - _id: PaSc - _id: GradSch doi: 10.5194/mr-7-29-2026 external_id: pmid: - '42057802' has_accepted_license: '1' intvolume: ' 7' issue: '1' language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.5194/mr-7-29-2026 month: '04' oa: 1 oa_version: Published Version page: 29-37 pmid: 1 project: - _id: B67AFEDC-15C9-11EA-A837-991A96BB2854 name: IST Austria Open Access Fund - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publication: Magnetic Resonance publication_identifier: eissn: - 2699-0016 publication_status: published publisher: Copernicus Publications quality_controlled: '1' related_material: record: - id: '22334' relation: dissertation_contains status: public scopus_import: '1' status: public title: Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 7 year: '2026' ... --- OA_type: closed access _id: '22638' abstract: - lang: eng text: The one-bond proton-carbon coupling constant (1JCH) is an insightful probe of carbohydrate configuration. Equatorial and axial protons at the C1 position typically exhibit distinct 1JCH values, enabling NMR measurements to distinguish α- and β-configurations in carbohydrates. In principle, such measurements could provide insights into carbohydrates in the cell walls of intact microbes. However, traditionally, these measurements are performed by solution NMR with carbohydrates that were extracted, solubilized and fractionated, leaving the biological relevance of the measurements uncertain. Here, we demonstrate that 1H-detected solid-state NMR with fast magic-angle spinning allows quantitative measurements of 1JCH couplings for mobile capsular polysaccharides, directly on submilligram amounts of pathogenic cells. Our approach is demonstrated on intact cells of the pathogenic yeast Cryptococcus neoformans. High-resolution proton-detected spectra enabled the determination of coupling constants for five mobile polysaccharide units of the cryptococcal capsule, revealing their native configurations and confirming previous solution NMR-based anomeric configuration assignments. acknowledgement: We thank the ANR (ANR-16-CE11-0020-02 to A. Loquet and V.A. and ANR-21-CE17-0032 to V.A.) as well as the Swiss National Science Foundation for early postdoc mobility project P2EZP2_184258 to A. Lends. This work has benefited from the Biophysical and Structural Chemistry Platform at Institut Européen de Chimie et Biologie IECB, Centre National de la Recherche Scientifique CNRS Unité d’Appui et de Recherche UAR 3033, INSERM US001, and the CNRS (IR-RMN FR3050 and Infranalytics FR2054). article_processing_charge: No article_type: original author: - first_name: Alons full_name: Lends, Alons last_name: Lends - first_name: Gaelle full_name: Lamon, Gaelle last_name: Lamon - first_name: Alicia full_name: Vallet, Alicia last_name: Vallet - first_name: Axelle full_name: Grélard, Axelle last_name: Grélard - first_name: Estelle full_name: Morvan, Estelle last_name: Morvan - first_name: Vishukumar full_name: Aimanianda, Vishukumar last_name: Aimanianda - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Antoine full_name: Loquet, Antoine last_name: Loquet citation: ama: Lends A, Lamon G, Vallet A, et al. On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR. Journal of the American Chemical Society. 2026;148(27):28037-28042. doi:10.1021/jacs.6c06064 apa: Lends, A., Lamon, G., Vallet, A., Grélard, A., Morvan, E., Aimanianda, V., … Loquet, A. (2026). On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.6c06064 chicago: Lends, Alons, Gaelle Lamon, Alicia Vallet, Axelle Grélard, Estelle Morvan, Vishukumar Aimanianda, Paul Schanda, and Antoine Loquet. “On-Cell Detection of Polysaccharide One-Bond1Jch Couplings by Proton-Detected Solid-State NMR.” Journal of the American Chemical Society. American Chemical Society, 2026. https://doi.org/10.1021/jacs.6c06064. ieee: A. Lends et al., “On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR,” Journal of the American Chemical Society, vol. 148, no. 27. American Chemical Society, pp. 28037–28042, 2026. ista: Lends A, Lamon G, Vallet A, Grélard A, Morvan E, Aimanianda V, Schanda P, Loquet A. 2026. On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR. Journal of the American Chemical Society. 148(27), 28037–28042. mla: Lends, Alons, et al. “On-Cell Detection of Polysaccharide One-Bond1Jch Couplings by Proton-Detected Solid-State NMR.” Journal of the American Chemical Society, vol. 148, no. 27, American Chemical Society, 2026, pp. 28037–42, doi:10.1021/jacs.6c06064. short: A. Lends, G. Lamon, A. Vallet, A. Grélard, E. Morvan, V. Aimanianda, P. Schanda, A. Loquet, Journal of the American Chemical Society 148 (2026) 28037–28042. das_tickbox: '0' date_created: 2026-08-03T13:20:41Z date_published: 2026-06-15T00:00:00Z date_updated: 2026-08-04T05:52:13Z day: '15' department: - _id: PaSc doi: 10.1021/jacs.6c06064 external_id: pmid: - '42377973' intvolume: ' 148' issue: '27' language: - iso: eng month: '06' oa_version: None page: 28037-28042 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' researchdata_availability: no scopus_import: '1' status: public supplementarymaterial: yes title: On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 148 year: '2026' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '22268' abstract: - lang: eng text: AlphaFold3 predicts highly accurate protein structures from sequence but tends to collapse to a single dominant conformation, even when the underlying structure is inherently heterogeneous. Moreover, its predictions are oblivious to experimental conditions that can alter local sequence conformation. In this work, we show that AlphaFold3 can be guided to match data obtained by nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography and cryogenic electron microscopy (cryo-EM) experiments and combinations thereof. Our approach can also incorporate data that explicitly report on dynamics, such as site-resolved order parameters. We demonstrate that this methodology generates compact structural ensembles whose ensemble-averaged observables agree with experiment, with fewer distance restraint violations than traditionally resolved NMR structures and with unmodeled alternate conformations uncovered in electron density. This methodology paves the way for experimentally aware predictive models that generate structural ensembles consistent with the measurements, potentially over multiple modalities, and that can be further refined toward thermodynamically grounded ensembles by incorporating energetics. acknowledgement: A. Marx acknowledges the financial support of the Helmsley Fellowships Program for Sustainability and Health. A.M.B. and P.S. are supported by the Institute of Science and Technology Austria Internal Project Call grant Generative Protein NMR. S.V. was supported in part by funding from the Eric and Wendy Schmidt Center at the Broad Institute of MIT and Harvard. Open access funding provided by Institute of Science and Technology (IST Austria). article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Sai A full_name: Maddipatla, Sai A id: e957f5e5-91c9-11f0-a95f-e090f66ecb4d last_name: Maddipatla - first_name: Nadav E full_name: Sellam, Nadav E id: ef280fe0-91c9-11f0-a95f-8dea3f5bc513 last_name: Sellam - first_name: Meital I full_name: Bojan, Meital I id: 11d88cf5-91ca-11f0-a95f-edf9f08f47b7 last_name: Bojan - first_name: Vova full_name: Masalitin, Vova id: ff7958eb-91c9-11f0-a95f-f3bf65828cf6 last_name: Masalitin - first_name: Sanketh full_name: Vedula, Sanketh last_name: Vedula - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Ailie full_name: Marx, Ailie last_name: Marx - first_name: Alexander full_name: Bronstein, Alexander id: 58f3726e-7cba-11ef-ad8b-e6e8cb3904e6 last_name: Bronstein orcid: 0000-0001-9699-8730 citation: ama: Maddipatla SA, Sellam NE, Bojan MI, et al. Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles. Nature Biotechnology. 2026. doi:10.1038/s41587-026-03166-5 apa: Maddipatla, S. A., Sellam, N. E., Bojan, M. I., Masalitin, V., Vedula, S., Schanda, P., … Bronstein, A. M. (2026). Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles. Nature Biotechnology. Springer Nature. https://doi.org/10.1038/s41587-026-03166-5 chicago: Maddipatla, Sai A, Nadav E Sellam, Meital I Bojan, Vova Masalitin, Sanketh Vedula, Paul Schanda, Ailie Marx, and Alex M. Bronstein. “Experiment-Guided AlphaFold3 Resolves Measurement-Consistent Protein Ensembles.” Nature Biotechnology. Springer Nature, 2026. https://doi.org/10.1038/s41587-026-03166-5. ieee: S. A. Maddipatla et al., “Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles,” Nature Biotechnology. Springer Nature, 2026. ista: Maddipatla SA, Sellam NE, Bojan MI, Masalitin V, Vedula S, Schanda P, Marx A, Bronstein AM. 2026. Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles. Nature Biotechnology. mla: Maddipatla, Sai A., et al. “Experiment-Guided AlphaFold3 Resolves Measurement-Consistent Protein Ensembles.” Nature Biotechnology, Springer Nature, 2026, doi:10.1038/s41587-026-03166-5. short: S.A. Maddipatla, N.E. Sellam, M.I. Bojan, V. Masalitin, S. Vedula, P. Schanda, A. Marx, A.M. Bronstein, Nature Biotechnology (2026). corr_author: '1' das_tickbox: '1' dataavailabilitystatement: All structures and metrics reported in this paper are openly available on Harvard Dataverse - https://doi.org/10.7910/DVN/PLYUHN. All code is openly available on GitHub (https://github.com/sai-advaith/guided_alphafold); the version used for this paper (version 0.9.1) is permanently archived on Zenodo https://doi.org/10.5281/zenodo.17307005 date_created: 2026-07-12T22:02:19Z date_published: 2026-06-29T00:00:00Z date_updated: 2026-08-04T09:25:18Z day: '29' ddc: - '570' department: - _id: PaSc - _id: AlBr - _id: GradSch doi: 10.1038/s41587-026-03166-5 external_id: pmid: - '42374114' has_accepted_license: '1' language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/s41587-026-03166-5 month: '06' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Biotechnology publication_identifier: eissn: - 1546-1696 issn: - 1087-0156 publication_status: epub_ahead publisher: Springer Nature quality_controlled: '1' related_material: link: - description: News on ISTA website relation: press_release url: https://ista.ac.at/en/news/toward-experiment-guided-alphafold/ researchdata_availability: yes scopus_import: '1' status: public supplementarymaterial: yes title: Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd year: '2026' ... --- OA_place: publisher _id: '22334' abstract: - lang: eng text: "Characterizing protein dynamics at the atomic level is essential for our understanding of biological mechanisms. Whether it is to facilitate metabolite transport, catalyze reactions, transmit signals, or regulate metabolism – proteins are constantly in motion and sample multiple conformational states to fulfill their function. Nuclear magnetic resonance (NMR) spectroscopy is particularly well suited to elucidate the dynamics of biomolecules on their complex free-energy landscape. In particular, solid-state magic-angle spinning (MAS) NMR enables the study of large molecular assemblies, protein crystals, or insoluble proteins at atomic resolution without an inherent molecular size limitation. MAS NMR experiments to probe protein dynamics are extremely versatile and sensitive to motional timescales from picoseconds to seconds. Over the past decades, technological advances, developments in experimental design, and new isotope-labeling approaches have further expanded the possibilities of this technique and significantly improved the accuracy of the determined motional parameters.\r\nFunctionally important sites of proteins often contain aromatic residues. Their side-chain motions have therefore long served as valuable indicators of mechanistically relevant dynamics in NMR studies. In this thesis, site-specifically labeled aromatic residues act as sensitive reporters for MAS NMR studies of protein dynamics. The first part addresses how different environments impact side-chain motion by probing ring flips of phenylalanines and tyrosines in crystalline proteins and amyloid fibrils. It provides important insights for the analysis of dynamics obtained in non-native protein environments and emphasizes the complex factors that determine the timescale of internal dynamics. In the second part, the focus shifts towards methodological questions regarding the investigation of protein dynamics by 19F MAS NMR. The fluorine nucleus exhibits promising characteristics for NMR studies but also presents significant challenges, which is why the full methodological potential of 19F MAS NMR has not been fully realized yet. This work demonstrates that paramagnetic doping can considerably reduce the measurement time and improve the sensitivity of fluorinated samples. Finally, 19F MAS NMR is evaluated as a tool for studying protein side-chain dynamics on the example of tryptophans. The results illustrate the challenges in analyzing such experiments and lay the foundation for further development of 19F MAS NMR relaxation studies.\r\nTaken together, this thesis highlights the potential of combining specific isotope labeling, MAS NMR, and complementary methods such as crystallography and computational simulations to elucidate internal protein dynamics. The further development of such integrative approaches will be crucial to improving our understanding of complex mechanisms and protein function.\r\n" acknowledged_ssus: - _id: LifeSc - _id: NMR acknowledgement: "During the work on this thesis, I was the recipient of a DOC Fellowship of the Austrian\r\nAcademy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01)." alternative_title: - ISTA Thesis article_processing_charge: No author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 citation: ama: Becker LM. Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR. 2026. doi:10.15479/AT-ISTA-22334 apa: Becker, L. M. (2026). Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR. Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-22334 chicago: Becker, Lea Marie. “Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR.” Institute of Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-22334. ieee: L. M. Becker, “Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR,” Institute of Science and Technology Austria, 2026. ista: Becker LM. 2026. Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR. Institute of Science and Technology Austria. mla: Becker, Lea Marie. Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR. Institute of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-22334. short: L.M. Becker, Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR, Institute of Science and Technology Austria, 2026. corr_author: '1' das_tickbox: '1' date_created: 2026-07-14T08:08:51Z date_published: 2026-07-13T00:00:00Z date_updated: 2026-08-04T09:32:45Z day: '13' ddc: - '572' degree_awarded: PhD department: - _id: GradSch - _id: PaSc doi: 10.15479/AT-ISTA-22334 doi_confirm: '1' file: - access_level: closed checksum: 8b85114eff543916c0e1445cd2189555 content_type: application/zip creator: lbecker date_created: 2026-07-16T09:17:08Z date_updated: 2026-07-16T09:17:08Z file_id: '22346' file_name: 2026_Becker_Lea_source_files.zip file_size: 99472908 relation: source_file - access_level: open_access checksum: 6c526862bc6dbd1e4c80ecb34580bc58 content_type: application/pdf creator: lbecker date_created: 2026-07-16T09:17:05Z date_updated: 2026-07-16T09:17:05Z file_id: '22347' file_name: 2026_Becker_Lea_Thesis.pdf file_size: 74647289 relation: main_file success: 1 file_date_updated: 2026-07-16T09:17:08Z has_accepted_license: '1' language: - iso: eng license: https://creativecommons.org/licenses/by-nc-nd/4.0/ month: '07' oa: 1 oa_version: Published Version page: '205' project: - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publication_identifier: isbn: - 978-3-99078-084-8 issn: - 2663-337X publication_status: published publisher: Institute of Science and Technology Austria related_material: record: - id: '12675' relation: part_of_dissertation status: public - id: '21777' relation: part_of_dissertation status: public - id: '12114' relation: part_of_dissertation status: public - id: '22105' relation: part_of_dissertation status: public status: public supervisor: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 title: Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: dissertation user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9 year: '2026' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '22105' abstract: - lang: eng text: Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein–protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labelling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a crystal structure of a GB1 variant reported in this work, reproduce these elevated barriers and reveal how the crystal restrains motions. acknowledged_ssus: - _id: NMR - _id: LifeSc 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). article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Haohao full_name: Fu, Haohao last_name: Fu - first_name: Benjamin full_name: Tatman, Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - first_name: Matthias full_name: Dreydoppel, Matthias last_name: Dreydoppel - first_name: Anna full_name: Kapitonova, Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - first_name: Daniel full_name: Balazs, Daniel id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E last_name: Balazs orcid: 0000-0001-7597-043X - first_name: Ulrich full_name: Weininger, Ulrich last_name: Weininger - first_name: Sylvain full_name: Engilberge, Sylvain last_name: Engilberge - first_name: Christophe full_name: Chipot, Christophe last_name: Chipot - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. Nature Chemistry. 2026;18:1221-1230. doi:10.1038/s41557-026-02155-0 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. Nature Chemistry. Springer Nature. https://doi.org/10.1038/s41557-026-02155-0 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.” Nature Chemistry. Springer Nature, 2026. https://doi.org/10.1038/s41557-026-02155-0. ieee: L. M. Becker et al., “Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes,” Nature Chemistry, vol. 18. Springer Nature, pp. 1221–1230, 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. 18, 1221–1230. mla: Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Nature Chemistry, vol. 18, Springer Nature, 2026, pp. 1221–30, doi:10.1038/s41557-026-02155-0. short: L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U. Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry 18 (2026) 1221–1230. corr_author: '1' das_tickbox: '1' 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. date_created: 2026-06-21T22:03:01Z date_published: 2026-07-01T00:00:00Z date_updated: 2026-08-04T09:32:45Z day: '01' ddc: - '540' department: - _id: PaSc - _id: LifeSc doi: 10.1038/s41557-026-02155-0 external_id: pmid: - '42271006' file: - access_level: open_access checksum: 1069fb27949fd2cb641b043b3a96a580 content_type: application/pdf creator: dernst date_created: 2026-07-28T06:58:35Z date_updated: 2026-07-28T06:58:35Z file_id: '22595' file_name: 2026_NatureChemistry_Becker.pdf file_size: 2618184 relation: main_file success: 1 file_date_updated: 2026-07-28T06:58:35Z has_accepted_license: '1' intvolume: ' 18' language: - iso: eng month: '07' oa: 1 oa_version: Published Version page: 1221-1230 pmid: 1 project: - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publication: Nature Chemistry publication_identifier: eissn: - '17554349' issn: - '17554330' publication_status: published publisher: Springer Nature quality_controlled: '1' related_material: link: - description: News on ISTA website relation: research_data url: https://ista.ac.at/en/news/how-proteins-breathe/ record: - id: '20641' relation: research_data status: public - id: '21145' relation: research_data status: public - id: '22334' relation: dissertation_contains status: public researchdata_availability: yes scopus_import: '1' status: public supplementarymaterial: yes title: Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd volume: 18 year: '2026' ... --- _id: '21145' 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. ' acknowledged_ssus: - _id: NMR - _id: LifeSc 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." article_processing_charge: No author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Christophe full_name: Chipot, Christophe last_name: Chipot citation: ama: Becker LM, Schanda P, Chipot C. Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2026. doi:10.15479/AT-ISTA-21145 apa: Becker, L. M., 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. https://doi.org/10.15479/AT-ISTA-21145 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. https://doi.org/10.15479/AT-ISTA-21145. 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. 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, 10.15479/AT-ISTA-21145. mla: Becker, Lea Marie, et al. Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-21145. short: L.M. Becker, P. Schanda, C. Chipot, (2026). contributor: - contributor_type: researcher first_name: Haohao last_name: Fu - contributor_type: researcher first_name: Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - contributor_type: researcher first_name: Matthias last_name: Dreydoppel - contributor_type: researcher first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: researcher first_name: Daniel id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E last_name: Balazs orcid: 0000-0001-7597-043X - contributor_type: researcher first_name: Ulrich last_name: Weininger - contributor_type: researcher first_name: Sylvain last_name: Engilberge corr_author: '1' date_created: 2026-02-05T13:54:39Z date_published: 2026-02-09T00:00:00Z date_updated: 2026-08-04T09:32:45Z day: '09' ddc: - '572' department: - _id: GradSch - _id: PaSc doi: 10.15479/AT-ISTA-21145 file: - access_level: open_access checksum: 02a419cce8cea450bc952f35488d2df5 content_type: text/plain creator: lbecker date_created: 2026-02-05T13:52:37Z date_updated: 2026-02-05T13:52:37Z file_id: '21146' file_name: README.txt file_size: 4263 relation: table_of_contents - access_level: open_access checksum: b0b82b1aa73985b0b308a3fa52d21aea content_type: application/zip creator: lbecker date_created: 2026-02-05T13:52:41Z date_updated: 2026-02-05T13:52:41Z file_id: '21147' file_name: Research_Data.zip file_size: 50647107 relation: main_file success: 1 file_date_updated: 2026-02-05T13:52:41Z has_accepted_license: '1' month: '02' oa: 1 oa_version: Published Version project: - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publisher: Institute of Science and Technology Austria related_material: record: - id: '20641' relation: earlier_version status: public - id: '22105' relation: used_in_publication status: public status: public title: Additional Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes" tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 year: '2026' ... --- OA_place: publisher OA_type: gold _id: '22722' abstract: - lang: eng text: "The local structure of a protein strongly impacts its function and interactions\r\nwith other molecules. Representing local biomolecular environments remains a\r\nkey challenge while applying machine learning approaches over protein structures. The structural and chemical variability of these environments makes them\r\nchallenging to model, and performing representation learning on these objects\r\nremains largely under-explored. In this work, we propose representations for\r\nlocal protein environments that leverage intermediate features from machine learning force fields (MLFFs). We extensively benchmark state-of-the-art MLFFs,\r\ncomparing their performance across latent spaces and downstream tasks, and\r\nshow that their embeddings capture local structural (e.g., secondary motifs) and\r\nchemical features (e.g., amino acid identity and protonation state), organizing\r\nprotein environments into a structured manifold. We show that these representations enable zero-shot generalization and transfer across diverse downstream\r\ntasks. As a case study, we build a physics-informed, uncertainty-aware chemical shift predictor that achieves state-of-the-art accuracy in biomolecular NMR\r\nspectroscopy. Our results establish MLFFs as general-purpose, reusable representation learners for protein modeling, opening new directions in representation learning for structured physical systems. Code and data are available at\r\nhttps://github.com/mb012/MLFF_representation.\r\n" acknowledged_ssus: - _id: ScienComp acknowledgement: "This work was supported by the Institute of Science and Technology Austria (ISTA) through the IPC\r\ngrant “Generative Protein NMR” and by the Israeli Science Foundation (ISF) under grant number\r\n1834/24. This research used resources of the Institute of Science and Technology Austria’s scientific\r\ncomputing cluster. S.V. was supported in part by funding from the Eric and Wendy Schmidt Center at\r\nthe Broad Institute of MIT and Harvard." article_processing_charge: No arxiv: 1 author: - first_name: Meital I full_name: Bojan, Meital I id: 11d88cf5-91ca-11f0-a95f-edf9f08f47b7 last_name: Bojan - first_name: Sanketh full_name: Vedula, Sanketh last_name: Vedula - first_name: Sai A full_name: Maddipatla, Sai A id: e957f5e5-91c9-11f0-a95f-e090f66ecb4d last_name: Maddipatla - first_name: Nadav E full_name: Sellam, Nadav E id: ef280fe0-91c9-11f0-a95f-8dea3f5bc513 last_name: Sellam - first_name: Anar full_name: Rzayev, Anar id: 2cd60677-9acd-11f1-ae1a-a85ae1c4dd35 last_name: Rzayev - first_name: Federico full_name: Napoli, Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Alexander full_name: Bronstein, Alexander id: 58f3726e-7cba-11ef-ad8b-e6e8cb3904e6 last_name: Bronstein orcid: 0000-0001-9699-8730 citation: ama: 'Bojan MI, Vedula S, Maddipatla SA, et al. Representing local protein environments with machine learning force fields. In: 14th International Conference on Learning Representations. Vol 2026. ; 2026:100760-100799.' apa: Bojan, M. I., Vedula, S., Maddipatla, S. A., Sellam, N. E., Rzayev, A., Napoli, F., … Bronstein, A. M. (2026). Representing local protein environments with machine learning force fields. In 14th International Conference on Learning Representations (Vol. 2026, pp. 100760–100799). Rio de Janeiro, Brazil. chicago: Bojan, Meital I, Sanketh Vedula, Sai A Maddipatla, Nadav E Sellam, Anar Rzayev, Federico Napoli, Paul Schanda, and Alex M. Bronstein. “Representing Local Protein Environments with Machine Learning Force Fields.” In 14th International Conference on Learning Representations, 2026:100760–99, 2026. ieee: M. I. Bojan et al., “Representing local protein environments with machine learning force fields,” in 14th International Conference on Learning Representations, Rio de Janeiro, Brazil, 2026, vol. 2026, pp. 100760–100799. ista: 'Bojan MI, Vedula S, Maddipatla SA, Sellam NE, Rzayev A, Napoli F, Schanda P, Bronstein AM. 2026. Representing local protein environments with machine learning force fields. 14th International Conference on Learning Representations. ICLR: International Conference on Learning Representations vol. 2026, 100760–100799.' mla: Bojan, Meital I., et al. “Representing Local Protein Environments with Machine Learning Force Fields.” 14th International Conference on Learning Representations, vol. 2026, 2026, pp. 100760–99. short: M.I. Bojan, S. Vedula, S.A. Maddipatla, N.E. Sellam, A. Rzayev, F. Napoli, P. Schanda, A.M. Bronstein, in:, 14th International Conference on Learning Representations, 2026, pp. 100760–100799. conference: end_date: 2026-04-27 location: Rio de Janeiro, Brazil name: 'ICLR: International Conference on Learning Representations' start_date: 2026-04-23 corr_author: '1' das_tickbox: '1' dataavailabilitystatement: "The code, trained models, and data-processing scripts are publicly available at https://github.\r\ncom/mb012/MLFF_representation. In addition, complete details of the models and optimization parameters are provided in Appendix G.3. The hardware resources used to produce the\r\nresults are specified in Appendix I.4. The loss functions, evaluation metrics, and details regarding\r\nablation studies are specified in Appendix G. These details ensure that all results reported in the paper\r\ncan be independently verified." date_created: 2026-08-17T12:03:24Z date_published: 2026-05-01T00:00:00Z date_updated: 2026-08-18T06:36:55Z day: '01' ddc: - '000' - '570' department: - _id: GradSch - _id: PaSc - _id: AlBr external_id: arxiv: - '2505.23354' file: - access_level: open_access checksum: 9f43f5469443388ec55388d95c4cf243 content_type: application/pdf creator: dernst date_created: 2026-08-18T06:33:14Z date_updated: 2026-08-18T06:33:14Z file_id: '22723' file_name: 2026_ICLR_Bojan.pdf file_size: 8534339 relation: main_file success: 1 file_date_updated: 2026-08-18T06:33:14Z has_accepted_license: '1' intvolume: ' 2026' language: - iso: eng month: '05' oa: 1 oa_version: Published Version page: 100760-100799 publication: 14th International Conference on Learning Representations publication_status: published quality_controlled: '1' related_material: link: - relation: software url: https://github.com/mb012/MLFF_representation researchdata_availability: yes status: public supplementarymaterial: yes title: Representing local protein environments with machine learning force fields tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: conference user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 2026 year: '2026' ... --- OA_place: repository _id: '22687' abstract: - lang: eng text: "Understanding enzyme function requires characterizing not only static structure but also dynamics and ligand interactions. NMR spectroscopy provides this insight at atomic resolution, yet for large proteins the difficulty of resonance assignment has largely confined such studies to systems below ∼50 kDa, or to observing only methyl groups. Here we present an integrated magic-angle spinning (MAS) and solution NMR study of the 134 kDa tetrameric malate dehydrogenase from Ignicoccus islandicus (IiMDH), an enzyme of particular interest as an evolutionary intermediate between allosteric lactate\r\ndehydrogenases and non-allosteric malate dehydrogenases. By combining high-dimensional (up to 4D) MAS NMR experiments on sedimented protein with solution NMR, we achieved 92% backbone heavy- atom assignment and 91% assignment of all Ile-δ1, Leu-δ1/-δ2, Val-γ1/-γ2, Met-ε and Thr-γ methyl groups. Building on these assignments, we use various probes of backbone and sidechain dynamics: elevated MAS NMR 15N rotating-frame relaxation (R1ρ) points to microsecond motions in functionally critical regions, including the catalytic loop and the mobile surface loop. Complementary methyl-axis order parameters from solution NMR identified additional flexible sites in the hydrophobic core. Chemical shift perturbation experiments upon addition of the substrate analogue oxamate, monitored via backbone 1H-15N TROSY, revealed both active-site contacts and responses in helices α2F and α3G, regions implicated in allosteric signal transmission. The integrated approach demonstrated here exploits the distinct strengths of MAS and solution NMR, and provides a comprehensive view of structure, dynamics, and substrate interactions in a large oligomeric enzyme that would not be accessible by either technique alone." acknowledged_ssus: - _id: NMR - _id: LifeSc acknowledgement: This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra Rovó, Megha Mohan and Margarita Valhondo Falcón for excellent support of the NMR facility. article_processing_charge: No author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Federico full_name: Napoli, Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X citation: ama: 'Schanda P, Napoli F. Data and scripts for: “Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.” 2026. doi:10.15479/AT-ISTA-22687' apa: 'Schanda, P., & Napoli, F. (2026). Data and scripts for: “Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-22687' chicago: 'Schanda, Paul, and Federico Napoli. “Data and Scripts for: ‘Integrated Solid/Solution NMR Assignment Allows Mapping Dynamics and Ligand Binding in a 134 KDa Enzyme.’” Institute of Science and Technology Austria, 2026. https://doi.org/10.15479/AT-ISTA-22687.' ieee: 'P. Schanda and F. Napoli, “Data and scripts for: ‘Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme.’” Institute of Science and Technology Austria, 2026.' ista: 'Schanda P, Napoli F. 2026. Data and scripts for: ‘Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme’, Institute of Science and Technology Austria, 10.15479/AT-ISTA-22687.' mla: 'Schanda, Paul, and Federico Napoli. Data and Scripts for: “Integrated Solid/Solution NMR Assignment Allows Mapping Dynamics and Ligand Binding in a 134 KDa Enzyme.” Institute of Science and Technology Austria, 2026, doi:10.15479/AT-ISTA-22687.' short: P. Schanda, F. Napoli, (2026). contributor: - contributor_type: researcher first_name: Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X - contributor_type: project_leader first_name: Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - contributor_type: project_member first_name: Rajkumar id: a3089acd-6806-11ee-bacc-f0c7d500ad20 last_name: Singh - contributor_type: project_member first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: project_member first_name: Virgil last_name: Aitenbichler - contributor_type: project_member first_name: Giorgia id: 334a5e40-8747-11f0-b671-ba1f5154b4b4 last_name: Toscano - contributor_type: data_collector first_name: Barbara last_name: Perrone corr_author: '1' date_created: 2026-08-12T16:12:19Z date_published: 2026-08-20T00:00:00Z date_updated: 2026-08-20T07:40:15Z day: '20' department: - _id: PaSc doi: 10.15479/AT-ISTA-22687 doi_confirm: '1' file: - access_level: open_access checksum: dd23db23f7e75bafad6c67381163c1e2 content_type: application/vnd.openxmlformats-officedocument.spreadsheetml.sheet creator: fnapoli date_created: 2026-08-18T07:13:26Z date_updated: 2026-08-18T07:13:26Z file_id: '22725' file_name: Pulse_parameters.xlsx file_size: 59096 relation: main_file success: 1 - access_level: open_access checksum: a7ad194d8d7f780725bc2c60c63d686d content_type: application/zip creator: fnapoli date_created: 2026-08-18T07:16:00Z date_updated: 2026-08-18T07:16:00Z file_id: '22726' file_name: Scripts_submission.zip file_size: 3591173 relation: main_file success: 1 - access_level: open_access checksum: dc099c298844973512ab224464964a1a content_type: application/zip creator: fnapoli date_created: 2026-08-18T07:15:59Z date_updated: 2026-08-18T07:15:59Z file_id: '22727' file_name: FLYA_runs.zip file_size: 28750919 relation: main_file success: 1 - access_level: open_access checksum: 04bcce8eb20c90089cbd2fb5e0c50a7f content_type: application/zip creator: fnapoli date_created: 2026-08-18T07:33:47Z date_updated: 2026-08-18T07:33:47Z file_id: '22728' file_name: spectra_Bruker.zip file_size: 3824856998 relation: main_file success: 1 - access_level: open_access checksum: 91c1161ca98632ed643d2b564395da5b content_type: application/zip creator: fnapoli date_created: 2026-08-18T08:03:33Z date_updated: 2026-08-18T08:03:33Z file_id: '22729' file_name: Titration_data.zip file_size: 17880653 relation: main_file success: 1 - access_level: open_access checksum: ca2cf03b82656ae2858931d4391a3158 content_type: text/plain creator: arashid date_created: 2026-08-20T07:35:05Z date_updated: 2026-08-20T07:35:05Z file_id: '22743' file_name: README.txt file_size: 868 relation: main_file success: 1 file_date_updated: 2026-08-20T07:35:05Z has_accepted_license: '1' month: '08' oa: 1 oa_version: None project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publisher: Institute of Science and Technology Austria status: public title: 'Data and scripts for: "Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme"' tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2026' ... --- OA_place: publisher OA_type: gold _id: '21327' abstract: - lang: eng 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. acknowledged_ssus: - _id: ScienComp 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. ' alternative_title: - PMLR article_processing_charge: No arxiv: 1 author: - first_name: Sai A full_name: Maddipatla, Sai A id: e957f5e5-91c9-11f0-a95f-e090f66ecb4d last_name: Maddipatla - first_name: Nadav E full_name: Sellam, Nadav E id: ef280fe0-91c9-11f0-a95f-8dea3f5bc513 last_name: Sellam - first_name: Meital I full_name: Bojan, Meital I id: 11d88cf5-91ca-11f0-a95f-edf9f08f47b7 last_name: Bojan - first_name: Sanketh full_name: Vedula, Sanketh id: 94f2fe44-70fa-11f0-b76b-92922c09452b last_name: Vedula - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Ailie full_name: Marx, Ailie last_name: Marx - first_name: Alexander full_name: Bronstein, Alexander id: 58f3726e-7cba-11ef-ad8b-e6e8cb3904e6 last_name: Bronstein orcid: 0000-0001-9699-8730 citation: ama: 'Maddipatla SA, Sellam NE, Bojan MI, et al. Inverse problems with experiment-guided AlphaFold. In: Proceedings of the 42nd International Conference on Machine Learning. Vol 267. ML Research Press; 2025:42366-42393.' apa: 'Maddipatla, S. A., Sellam, N. E., Bojan, M. I., Vedula, S., Schanda, P., Marx, A., & Bronstein, A. M. (2025). Inverse problems with experiment-guided AlphaFold. In Proceedings of the 42nd International Conference on Machine Learning (Vol. 267, pp. 42366–42393). Vancouver, Canada: ML Research Press.' 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 Proceedings of the 42nd International Conference on Machine Learning, 267:42366–93. ML Research Press, 2025. ieee: S. A. Maddipatla et al., “Inverse problems with experiment-guided AlphaFold,” in Proceedings of the 42nd International Conference on Machine Learning, 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.' mla: Maddipatla, Sai A., et al. “Inverse Problems with Experiment-Guided AlphaFold.” Proceedings of the 42nd International Conference on Machine Learning, vol. 267, ML Research Press, 2025, pp. 42366–93. 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. conference: end_date: 2025-07-19 location: Vancouver, Canada name: 'ICML: International Conference on Machine Learning' start_date: 2025-07-13 corr_author: '1' date_created: 2026-02-18T12:11:17Z date_published: 2025-07-30T00:00:00Z date_updated: 2026-02-19T08:56:43Z day: '30' ddc: - '000' - '540' department: - _id: PaSc - _id: AlBr - _id: GradSch external_id: arxiv: - '2502.09372' file: - access_level: open_access checksum: f33230a6d59b7978d4cd72795e4e9059 content_type: application/pdf creator: dernst date_created: 2026-02-19T08:56:10Z date_updated: 2026-02-19T08:56:10Z file_id: '21338' file_name: 2025_ICML_Maddipatla.pdf file_size: 1924177 relation: main_file success: 1 file_date_updated: 2026-02-19T08:56:10Z has_accepted_license: '1' intvolume: ' 267' language: - iso: eng month: '07' oa: 1 oa_version: Published Version page: 42366 - 42393 project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery - _id: bdb9578d-d553-11ed-ba76-ed5d39fce6f0 grant_number: I06223 name: Structure and mechanism of the mitochondrial MIM insertase publication: Proceedings of the 42nd International Conference on Machine Learning publication_identifier: eissn: - 2640-3498 publication_status: published publisher: ML Research Press quality_controlled: '1' status: public title: Inverse problems with experiment-guided AlphaFold tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: conference user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 267 year: '2025' ... --- OA_type: closed access _id: '19072' abstract: - lang: eng 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. 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). article_processing_charge: No article_type: original author: - first_name: Alons full_name: Lends, Alons last_name: Lends - first_name: Gaelle full_name: Lamon, Gaelle last_name: Lamon - first_name: Loic full_name: Delcourte, Loic last_name: Delcourte - first_name: Aude full_name: Sturny-Leclere, Aude last_name: Sturny-Leclere - first_name: Axelle full_name: Grélard, Axelle last_name: Grélard - first_name: Estelle full_name: Morvan, Estelle last_name: Morvan - first_name: Muhammed Bilal full_name: Abdul-Shukkoor, Muhammed Bilal last_name: Abdul-Shukkoor - first_name: Mélanie full_name: Berbon, Mélanie last_name: Berbon - first_name: Alicia full_name: Vallet, Alicia last_name: Vallet - first_name: Birgit full_name: Habenstein, Birgit last_name: Habenstein - first_name: Erick J. full_name: Dufourc, Erick J. last_name: Dufourc - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Vishukumar full_name: Aimanianda, Vishukumar last_name: Aimanianda - first_name: Antoine full_name: Loquet, Antoine last_name: Loquet 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. Journal of the American Chemical Society. 2025;147(8):6813-6824. doi:10.1021/jacs.4c16975 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. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.4c16975 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.” Journal of the American Chemical Society. American Chemical Society, 2025. https://doi.org/10.1021/jacs.4c16975. ieee: A. Lends et al., “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, 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. mla: Lends, Alons, et al. “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, vol. 147, no. 8, American Chemical Society, 2025, pp. 6813–24, doi:10.1021/jacs.4c16975. 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. date_created: 2025-02-23T23:01:56Z date_published: 2025-02-16T00:00:00Z date_updated: 2025-09-30T10:36:53Z day: '16' department: - _id: PaSc doi: 10.1021/jacs.4c16975 external_id: isi: - '001423628600001' pmid: - '39955787' intvolume: ' 147' isi: 1 issue: '8' language: - iso: eng month: '02' oa_version: None page: 6813-6824 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 147 year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '19555' abstract: - lang: eng 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. acknowledged_ssus: - _id: NMR 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. article_number: e202500408 article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Darja full_name: Rohden, Darja id: 81dc668a-19fa-11f0-bf31-d56534059ef3 last_name: Rohden - first_name: Giorgia full_name: Toscano, Giorgia last_name: Toscano - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Roman J. full_name: Lichtenecker, Roman J. last_name: Lichtenecker 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. Chemistry - A European Journal. 2025;31(24). doi:10.1002/chem.202500408 apa: Rohden, D., Toscano, G., Schanda, P., & Lichtenecker, R. J. (2025). Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy. Chemistry - A European Journal. Wiley. https://doi.org/10.1002/chem.202500408 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.” Chemistry - A European Journal. Wiley, 2025. https://doi.org/10.1002/chem.202500408. 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,” Chemistry - A European Journal, 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. mla: Rohden, Darja, et al. “Synthesis of Selectively 13C/2H/15N- Labeled Arginine to Probe Protein Conformation and Interaction by NMR Spectroscopy.” Chemistry - A European Journal, vol. 31, no. 24, e202500408, Wiley, 2025, doi:10.1002/chem.202500408. short: D. Rohden, G. Toscano, P. Schanda, R.J. Lichtenecker, Chemistry - A European Journal 31 (2025). corr_author: '1' date_created: 2025-04-13T22:01:19Z date_published: 2025-04-25T00:00:00Z date_updated: 2025-09-30T11:35:05Z day: '25' ddc: - '540' department: - _id: PaSc doi: 10.1002/chem.202500408 external_id: isi: - '001479486400019' pmid: - '40080421' file: - access_level: open_access checksum: e3788628644b5aac666cf079b05f8fa7 content_type: application/pdf creator: dernst date_created: 2025-08-05T12:59:24Z date_updated: 2025-08-05T12:59:24Z file_id: '20136' file_name: 2025_ChemistryEur_Rohden.pdf file_size: 2840681 relation: main_file success: 1 file_date_updated: 2025-08-05T12:59:24Z has_accepted_license: '1' intvolume: ' 31' isi: 1 issue: '24' language: - iso: eng month: '04' oa: 1 oa_version: Published Version pmid: 1 project: - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publication: Chemistry - A European Journal publication_identifier: eissn: - 1521-3765 issn: - 0947-6539 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 31 year: '2025' ... --- _id: '19696' acknowledged_ssus: - _id: NMR - _id: LifeSc article_processing_charge: No author: - first_name: Benjamin full_name: Tatman, Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman citation: ama: 'Tatman B. Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” 2025. doi:10.15479/AT-ISTA-19696' 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. https://doi.org/10.15479/AT-ISTA-19696' 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. https://doi.org/10.15479/AT-ISTA-19696.' 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, 10.15479/AT-ISTA-19696.' mla: '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, doi:10.15479/AT-ISTA-19696.' short: B. Tatman, (2025). 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 - contributor_type: researcher first_name: Matthias last_name: Ernst - contributor_type: researcher first_name: Petra id: c316e53f-b965-11eb-b128-bb26acc59c00 last_name: Rovo orcid: 0000-0001-8729-7326 corr_author: '1' date_created: 2025-05-14T10:46:07Z date_published: 2025-07-31T00:00:00Z date_updated: 2026-06-10T08:33:41Z day: '31' department: - _id: PaSc doi: 10.15479/AT-ISTA-19696 file: - access_level: open_access checksum: 4c2d29404e070bda7d5619f728ec555c content_type: application/zip creator: btatman date_created: 2025-07-31T08:14:40Z date_updated: 2025-07-31T08:14:40Z file_id: '20094' file_name: dataset.zip file_size: 557878455 relation: main_file success: 1 - access_level: open_access checksum: 6cbccd602be0ecb6ddb1f81fdfcadf92 content_type: text/plain creator: btatman date_created: 2025-07-31T08:14:21Z date_updated: 2025-07-31T08:14:21Z file_id: '20095' file_name: readme.txt file_size: 3514 relation: main_file success: 1 file_date_updated: 2025-07-31T08:14:40Z has_accepted_license: '1' license: https://creativecommons.org/licenses/by-nc-sa/4.0/ month: '07' oa: 1 oa_version: Published Version publisher: Institute of Science and Technology Austria related_material: link: - description: Paper to which the dataset corresponds. relation: research_paper url: http.//doi.org/10.1021/jacs.5c09057 record: - id: '20321' relation: research_data status: public status: public title: 'Dataset for "Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State"' tmp: image: /images/cc_by_nc_sa.png legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) short: CC BY-NC-SA (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2025' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '20184' 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. 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" article_number: '1148' article_processing_charge: Yes article_type: original author: - first_name: Sofía D. full_name: Castell, Sofía D. last_name: Castell - first_name: Consuelo M. full_name: Fernandez, Consuelo M. last_name: Fernandez - first_name: Ignacio N. full_name: Tumas, Ignacio N. last_name: Tumas - first_name: Lucía M. full_name: Margara, Lucía M. last_name: Margara - first_name: Maria C full_name: Miserendino, Maria C id: 273e0cbd-72f0-11ef-b75a-f9f932e292fa last_name: Miserendino - first_name: Danilo G. full_name: Ceschin, Danilo G. last_name: Ceschin - first_name: Roberto J. full_name: Pezza, Roberto J. last_name: Pezza - first_name: Mariela R. full_name: Monti, Mariela R. last_name: Monti citation: ama: Castell SD, Fernandez CM, Tumas IN, et al. The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa. Communications Biology. 2025;8. doi:10.1038/s42003-025-08589-5 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. Communications Biology. Springer Nature. https://doi.org/10.1038/s42003-025-08589-5 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.” Communications Biology. Springer Nature, 2025. https://doi.org/10.1038/s42003-025-08589-5. ieee: S. D. Castell et al., “The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa,” Communications Biology, vol. 8. Springer Nature, 2025. 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. mla: Castell, Sofía D., et al. “The Low-Fidelity DNA Pol IV Accelerates Evolution of Pathogenicity Genes in Pseudomonas Aeruginosa.” Communications Biology, vol. 8, 1148, Springer Nature, 2025, doi:10.1038/s42003-025-08589-5. 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). date_created: 2025-08-17T22:01:35Z date_published: 2025-08-02T00:00:00Z date_updated: 2025-09-30T14:18:46Z day: '02' ddc: - '570' department: - _id: PaSc - _id: GradSch doi: 10.1038/s42003-025-08589-5 external_id: isi: - '001541878500001' pmid: - '40753298' has_accepted_license: '1' intvolume: ' 8' isi: 1 language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/s42003-025-08589-5 month: '08' oa: 1 oa_version: Published Version pmid: 1 publication: Communications Biology publication_identifier: eissn: - 2399-3642 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 8 year: '2025' ... --- _id: '20242' 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 author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Schanda P. Data of: “Quantifying the carbon footprint of conference travel: the case of NMR meetings.” 2025. doi:10.15479/AT-ISTA-20242' apa: 'Schanda, P. (2025). Data of: “Quantifying the carbon footprint of conference travel: the case of NMR meetings.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20242' chicago: 'Schanda, Paul. “Data of: ‘Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.’” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-20242.' 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, 10.15479/AT-ISTA-20242.' mla: 'Schanda, Paul. Data of: “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.” Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-20242.' short: P. Schanda, (2025). contributor: - contributor_type: researcher first_name: Natalia id: D2761128-D73D-11E9-A1BF-BA0DE6697425 last_name: Ruzickova - contributor_type: researcher first_name: Lucky id: 84b9700b-15b2-11ec-abd3-831089e67615 last_name: Kapoor - contributor_type: researcher first_name: Valentin id: 4c665ce3-0016-11ec-bea0-e44de7a4fa3d last_name: Leitner - contributor_type: researcher first_name: Predrag id: 68AA0E5A-AFDA-11E9-9994-141DE6697425 last_name: Zivadinovic - contributor_type: researcher first_name: Maria A id: 44A03D04-AEA4-11E9-B225-EA2DE6697425 last_name: Sisak - contributor_type: researcher first_name: Cecelia N id: 2a69ab4b-896a-11ed-bdf8-cb8641cf2b21 last_name: Mweka - contributor_type: supervisor first_name: Jeroen A id: c15a5412-de82-11ed-b809-8dc1aa996e40 last_name: Dobbelaere - contributor_type: supervisor first_name: Georgios id: 38DB5788-F248-11E8-B48F-1D18A9856A87 last_name: Katsaros orcid: 0000-0001-8342-202X corr_author: '1' date_created: 2025-08-31T15:14:18Z date_published: 2025-09-01T00:00:00Z date_updated: 2026-06-10T08:45:12Z department: - _id: PaSc doi: 10.15479/AT-ISTA-20242 file: - access_level: open_access checksum: 055044b03f835cb98c45d0504f1db96e content_type: application/zip creator: pschanda date_created: 2025-08-31T15:09:44Z date_updated: 2025-08-31T15:09:44Z file_id: '20244' file_name: Abstracts.zip file_size: 42368943 relation: main_file success: 1 - access_level: open_access checksum: 1492683af736ac65088b77e12b52c3b0 content_type: application/zip creator: pschanda date_created: 2025-08-31T15:11:58Z date_updated: 2025-08-31T15:11:58Z file_id: '20245' file_name: data_CO2_conferences.zip file_size: 470659 relation: main_file success: 1 - access_level: open_access checksum: 8ac69071f7508e77b5ca91fa5018339a content_type: application/zip creator: pschanda date_created: 2025-08-31T15:12:03Z date_updated: 2025-08-31T15:12:03Z file_id: '20246' file_name: Figure6_predictions.zip file_size: 1138772 relation: main_file success: 1 - access_level: open_access checksum: 19b77db247feecdc36fbe6f68d94a76d content_type: text/x-python-script creator: pschanda date_created: 2025-08-31T15:12:07Z date_updated: 2025-08-31T15:12:07Z file_id: '20247' file_name: ExcelFileAnalysisCode.py file_size: 6558 relation: main_file success: 1 - access_level: open_access checksum: 39655e28c6df523f4f9662dc58c94623 content_type: application/pdf creator: pschanda date_created: 2025-08-31T15:12:11Z date_updated: 2025-08-31T15:12:11Z file_id: '20248' file_name: emissions_spectrometers_and_Parisgoal.pdf file_size: 1107467 relation: main_file success: 1 - access_level: open_access checksum: 2e9a9460b3f2abe7e46179561a63492b content_type: application/octet-stream creator: pschanda date_created: 2025-09-01T11:05:27Z date_updated: 2025-09-01T11:05:27Z file_id: '20263' file_name: README file_size: 3994 relation: main_file success: 1 file_date_updated: 2025-09-01T11:05:27Z has_accepted_license: '1' keyword: - sustainability - conference travel month: '09' oa: 1 oa_version: Published Version publisher: Institute of Science and Technology Austria related_material: record: - id: '20664' relation: used_in_publication status: public status: public title: 'Data of: "Quantifying the carbon footprint of conference travel: the case of NMR meetings"' tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '20321' 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. acknowledged_ssus: - _id: NMR - _id: LifeSc 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. article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Benjamin full_name: Tatman, Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - first_name: Vidhyalakshmi full_name: Sridharan, Vidhyalakshmi last_name: Sridharan - first_name: Motilal full_name: Uttarkabat, Motilal last_name: Uttarkabat - first_name: Christopher P. full_name: Jaroniec, Christopher P. last_name: Jaroniec - first_name: Matthias full_name: Ernst, Matthias last_name: Ernst - first_name: Petra full_name: Rovo, Petra id: c316e53f-b965-11eb-b128-bb26acc59c00 last_name: Rovo orcid: 0000-0001-8729-7326 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Tatman B, Sridharan V, Uttarkabat M, et al. Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. Journal of the American Chemical Society. 2025;147(32):29315-29326. doi:10.1021/jacs.5c09057' apa: 'Tatman, B., Sridharan, V., Uttarkabat, M., Jaroniec, C. P., 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. American Chemical Society. https://doi.org/10.1021/jacs.5c09057' 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.” Journal of the American Chemical Society. American Chemical Society, 2025. https://doi.org/10.1021/jacs.5c09057.' ieee: 'B. Tatman et al., “Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR,” Journal of the American Chemical Society, vol. 147, no. 32. American Chemical Society, pp. 29315–29326, 2025.' ista: 'Tatman B, Sridharan V, Uttarkabat M, Jaroniec CP, Ernst M, Rovo P, Schanda P. 2025. Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. Journal of the American Chemical Society. 147(32), 29315–29326.' mla: 'Tatman, Benjamin, et al. “Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” Journal of the American Chemical Society, vol. 147, no. 32, American Chemical Society, 2025, pp. 29315–26, doi:10.1021/jacs.5c09057.' 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. corr_author: '1' date_created: 2025-09-10T05:37:19Z date_published: 2025-08-01T00:00:00Z date_updated: 2026-06-10T08:33:41Z day: '01' ddc: - '540' department: - _id: PaSc - _id: NMR doi: 10.1021/jacs.5c09057 external_id: isi: - '001542746200001' pmid: - '40748291' file: - access_level: open_access checksum: b350d56ddddefea96cebd62c277c0ff5 content_type: application/pdf creator: dernst date_created: 2025-09-10T07:53:10Z date_updated: 2025-09-10T07:53:10Z file_id: '20337' file_name: 2025_JACS_Tatman.pdf file_size: 5235353 relation: main_file success: 1 file_date_updated: 2025-09-10T07:53:10Z has_accepted_license: '1' intvolume: ' 147' isi: 1 issue: '32' language: - iso: eng month: '08' oa: 1 oa_version: Published Version page: 29315-29326 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' related_material: record: - id: '19696' relation: used_in_publication status: public scopus_import: '1' status: public title: 'Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 147 year: '2025' ... --- APC_amount: 1260 EUR DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '20664' abstract: - lang: eng 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. 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).' article_processing_charge: Yes article_type: original author: - first_name: Lucky full_name: Kapoor, Lucky id: 84b9700b-15b2-11ec-abd3-831089e67615 last_name: Kapoor orcid: 0000-0001-8319-2148 - first_name: Natalia full_name: Ruzickova, Natalia id: D2761128-D73D-11E9-A1BF-BA0DE6697425 last_name: Ruzickova - first_name: Predrag full_name: Zivadinovic, Predrag id: 68AA0E5A-AFDA-11E9-9994-141DE6697425 last_name: Zivadinovic - first_name: Valentin full_name: Leitner, Valentin id: 4c665ce3-0016-11ec-bea0-e44de7a4fa3d last_name: Leitner - first_name: Maria A full_name: Sisak, Maria A id: 44A03D04-AEA4-11E9-B225-EA2DE6697425 last_name: Sisak - first_name: Cecelia N full_name: Mweka, Cecelia N id: 2a69ab4b-896a-11ed-bdf8-cb8641cf2b21 last_name: Mweka - first_name: Jeroen A full_name: Dobbelaere, Jeroen A id: c15a5412-de82-11ed-b809-8dc1aa996e40 last_name: Dobbelaere - first_name: Georgios full_name: Katsaros, Georgios id: 38DB5788-F248-11E8-B48F-1D18A9856A87 last_name: Katsaros orcid: 0000-0001-8342-202X - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: 'Kapoor L, Ruzickova N, Zivadinovic P, et al. Quantifying the carbon footprint of conference travel: The case of NMR meetings. Magnetic Resonance. 2025;6(2):243-256. doi:10.5194/mr-6-243-2025' 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. Magnetic Resonance. Copernicus Publications. https://doi.org/10.5194/mr-6-243-2025' 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.” Magnetic Resonance. Copernicus Publications, 2025. https://doi.org/10.5194/mr-6-243-2025.' ieee: 'L. Kapoor et al., “Quantifying the carbon footprint of conference travel: The case of NMR meetings,” Magnetic Resonance, vol. 6, no. 2. Copernicus Publications, pp. 243–256, 2025.' ista: 'Kapoor L, Ruzickova N, Zivadinovic P, Leitner V, Sisak MA, Mweka CN, Dobbelaere JA, Katsaros G, Schanda P. 2025. Quantifying the carbon footprint of conference travel: The case of NMR meetings. Magnetic Resonance. 6(2), 243–256.' mla: 'Kapoor, Lucky, et al. “Quantifying the Carbon Footprint of Conference Travel: The Case of NMR Meetings.” Magnetic Resonance, vol. 6, no. 2, Copernicus Publications, 2025, pp. 243–56, doi:10.5194/mr-6-243-2025.' 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. corr_author: '1' date_created: 2025-11-23T23:01:39Z date_published: 2025-11-10T00:00:00Z date_updated: 2026-06-10T08:45:11Z day: '10' ddc: - '000' department: - _id: JoFi - _id: GaTk - _id: JoCs - _id: EvBe - _id: TaHa - _id: GradSch - _id: GeKa - _id: PaSc doi: 10.5194/mr-6-243-2025 file: - access_level: open_access checksum: c63dd47b0e77f9451821436bb77d27c9 content_type: application/pdf creator: dernst date_created: 2025-11-24T08:25:19Z date_updated: 2025-11-24T08:25:19Z file_id: '20672' file_name: 2025_MagneticResonance_Kapoor.pdf file_size: 3081399 relation: main_file success: 1 file_date_updated: 2025-11-24T08:25:19Z has_accepted_license: '1' intvolume: ' 6' issue: '2' language: - iso: eng month: '11' oa: 1 oa_version: Published Version page: 243-256 project: - _id: B67AFEDC-15C9-11EA-A837-991A96BB2854 name: IST Austria Open Access Fund publication: Magnetic Resonance publication_identifier: eissn: - 2699-0016 publication_status: published publisher: Copernicus Publications quality_controlled: '1' related_material: link: - description: News on ISTA website relation: research_data url: https://ista.ac.at/en/news/carbon-footprint-of-conference-travel/ record: - id: '20242' relation: research_data status: public scopus_import: '1' status: public title: 'Quantifying the carbon footprint of conference travel: The case of NMR meetings' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 6 year: '2025' ... --- _id: '20641' 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. ' acknowledged_ssus: - _id: NMR - _id: LifeSc 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." article_processing_charge: No author: - first_name: Lea Marie full_name: Becker, Lea Marie id: 36336939-eb97-11eb-a6c2-c83f1214ca79 last_name: Becker orcid: 0000-0002-6401-5151 - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Becker LM, Schanda P. Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2025. doi:10.15479/AT-ISTA-20641 apa: Becker, L. M., & Schanda, P. (2025). Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20641 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. https://doi.org/10.15479/AT-ISTA-20641. 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, 10.15479/AT-ISTA-20641. mla: 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, doi:10.15479/AT-ISTA-20641. short: L.M. Becker, P. Schanda, (2025). contributor: - contributor_type: researcher first_name: 'Haohao ' last_name: Fu - contributor_type: researcher first_name: Benjamin id: 71cda2f3-e604-11ee-a1df-da10587eda3f last_name: Tatman - contributor_type: researcher first_name: Matthias last_name: Dreydoppel - contributor_type: researcher first_name: Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - contributor_type: researcher first_name: Daniel id: 302BADF6-85FC-11EA-9E3B-B9493DDC885E last_name: Balazs orcid: 0000-0001-7597-043X - contributor_type: researcher first_name: Ulrich last_name: Weininger - contributor_type: researcher first_name: Sylvain last_name: Engilberge - contributor_type: researcher first_name: Christophe last_name: Chipot corr_author: '1' date_created: 2025-11-13T09:29:58Z date_published: 2025-11-18T00:00:00Z date_updated: 2026-08-04T09:32:44Z day: '18' ddc: - '572' department: - _id: GradSch - _id: PaSc doi: 10.15479/AT-ISTA-20641 file: - access_level: open_access checksum: a73a0550c644957e7f62241e239d3a1d content_type: application/zip creator: lbecker date_created: 2025-11-13T09:38:35Z date_updated: 2026-02-17T10:16:57Z file_id: '20643' file_name: Research_Data.zip file_size: 1806589513 relation: main_file - access_level: open_access checksum: 7176b257f753c213a0460ee06f802363 content_type: application/pdf creator: lbecker date_created: 2025-11-17T11:54:17Z date_updated: 2026-02-17T10:16:57Z file_id: '20652' file_name: README.pdf file_size: 191376 relation: table_of_contents file_date_updated: 2026-02-17T10:16:57Z has_accepted_license: '1' month: '11' oa: 1 oa_version: Published Version project: - _id: 7be609c4-9f16-11ee-852c-85015ce2b9b0 grant_number: '26777' name: Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches publisher: Institute of Science and Technology Austria related_material: record: - id: '21145' relation: later_version status: public - id: '22105' relation: used_in_publication status: public status: public title: Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes" tmp: image: /images/cc_by_nc.png legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) short: CC BY-NC (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2025' ... --- OA_place: publisher OA_type: hybrid PlanS_conform: '1' _id: '20538' 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. acknowledged_ssus: - _id: NMR - _id: LifeSc 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. article_number: '169465' article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Sonja full_name: Knödlstorfer, Sonja last_name: Knödlstorfer - first_name: Giorgia full_name: Toscano, Giorgia id: 334a5e40-8747-11f0-b671-ba1f5154b4b4 last_name: Toscano - first_name: Aleksandra L. full_name: Ptaszek, Aleksandra L. last_name: Ptaszek - first_name: Georg full_name: Kontaxis, Georg last_name: Kontaxis - first_name: Federico full_name: Napoli, Federico id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b last_name: Napoli orcid: 0000-0002-9043-136X - first_name: Jakob full_name: Schneider, Jakob id: 64368429-eb97-11eb-a6c2-c980b1f44415 last_name: Schneider - first_name: Katharina full_name: Maier, Katharina last_name: Maier - first_name: Anna full_name: Kapitonova, Anna id: 9fb2a840-89e1-11ee-a8b7-cc5c7ba62471 last_name: Kapitonova - first_name: Roman J. full_name: Lichtenecker, Roman J. last_name: Lichtenecker - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Robert full_name: Konrat, Robert last_name: Konrat citation: 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. Journal of Molecular Biology. 2025;437(23). doi:10.1016/j.jmb.2025.169465 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. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2025.169465 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.” Journal of Molecular Biology. Elsevier, 2025. https://doi.org/10.1016/j.jmb.2025.169465. ieee: S. Knödlstorfer et al., “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, 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. 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.” Journal of Molecular Biology, vol. 437, no. 23, 169465, Elsevier, 2025, doi:10.1016/j.jmb.2025.169465. 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). date_created: 2025-10-26T23:01:35Z date_published: 2025-12-01T00:00:00Z date_updated: 2026-08-13T14:19:02Z day: '01' ddc: - '540' department: - _id: PaSc - _id: GradSch doi: 10.1016/j.jmb.2025.169465 external_id: pmid: - '41016549' file: - access_level: open_access checksum: feb92f9c79032c261165f4ca573f444a content_type: application/pdf creator: dernst date_created: 2025-12-30T10:29:08Z date_updated: 2025-12-30T10:29:08Z file_id: '20915' file_name: 2025_JourMolecularBiology_Knoedlstorfer.pdf file_size: 3076611 relation: main_file success: 1 file_date_updated: 2025-12-30T10:29:08Z has_accepted_license: '1' intvolume: ' 437' issue: '23' language: - iso: eng month: '12' oa: 1 oa_version: Published Version pmid: 1 project: - _id: bdb9578d-d553-11ed-ba76-ed5d39fce6f0 grant_number: I06223 name: Structure and mechanism of the mitochondrial MIM insertase - _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf grant_number: I05812 name: AlloSpace. The emergence and mechanisms of allostery publication: Journal of Molecular Biology publication_identifier: eissn: - 1089-8638 issn: - 0022-2836 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0 tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 437 year: '2025' ...