[{"day":"01","status":"public","OA_type":"hybrid","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"PlanS_conform":"1","citation":{"chicago":"Becker, Lea Marie, Haohao Fu, Benjamin Tatman, Matthias Dreydoppel, Anna Kapitonova, Daniel Balazs, Ulrich Weininger, Sylvain Engilberge, Christophe Chipot, and Paul Schanda. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>.","apa":"Becker, L. M., Fu, H., Tatman, B., Dreydoppel, M., Kapitonova, A., Balazs, D., … Schanda, P. (2026). Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>","mla":"Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>, vol. 18, Springer Nature, 2026, pp. 1221–30, doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>.","ieee":"L. M. Becker <i>et al.</i>, “Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes,” <i>Nature Chemistry</i>, vol. 18. Springer Nature, pp. 1221–1230, 2026.","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.","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.","ama":"Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. 2026;18:1221-1230. doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>"},"project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","grant_number":"26777","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0"}],"_id":"22105","scopus_import":"1","article_type":"original","intvolume":"        18","oa_version":"Published Version","type":"journal_article","acknowledgement":"We thank N. R. Skrynnikov and O. O. Lebedenko (St. Petersburg) for insightful discussions and for performing exploratory MD simulations. We are grateful to T. Schubeis (Lyon) for advice on GB1 crystallization and R. Schmid for initial crystallization trials. We thank C. Mueller-Dieckmann for assistance with room-temperature X-ray crystallography data collection on beamline ID30B at the ESRF, which is acknowledged for providing beamtime through its In-House Research programme. We thank S. Falkner for assistance with constructing the structural model of the IgG:GB1 complex. We thank J. Lewandowski for providing feedback on the paper and granting access to backbone relaxation data of IgG:GB1T2Q and GB1T2Q microcrystals. This research was supported by the Scientific Service Units (SSU) of the Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank P. Rovó and M. V. Falcón for excellent support of the NMR facility. L.M.B. is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant number PR10660EAW01). C.C. acknowledges the European Research Council (grant project 101097272 ‘MilliInMicro’) and the Métropole du Grand Nancy (grant project ‘ARC’). BM07-FIP2 is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under grant agreement ANR-21-ESRE-0011.Open access funding provided by Institute of Science and Technology (IST Austria).","month":"07","language":[{"iso":"eng"}],"date_published":"2026-07-01T00:00:00Z","department":[{"_id":"PaSc"},{"_id":"LifeSc"}],"publisher":"Springer Nature","date_updated":"2026-08-04T09:32:45Z","oa":1,"file_date_updated":"2026-07-28T06:58:35Z","doi":"10.1038/s41557-026-02155-0","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.","publication_identifier":{"issn":["17554330"],"eissn":["17554349"]},"publication":"Nature Chemistry","das_tickbox":"1","year":"2026","date_created":"2026-06-21T22:03:01Z","researchdata_availability":"yes","has_accepted_license":"1","ddc":["540"],"corr_author":"1","supplementarymaterial":"yes","file":[{"creator":"dernst","success":1,"content_type":"application/pdf","file_name":"2026_NatureChemistry_Becker.pdf","date_created":"2026-07-28T06:58:35Z","file_size":2618184,"date_updated":"2026-07-28T06:58:35Z","checksum":"1069fb27949fd2cb641b043b3a96a580","relation":"main_file","access_level":"open_access","file_id":"22595"}],"quality_controlled":"1","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"related_material":{"record":[{"status":"public","relation":"research_data","id":"20641"},{"status":"public","id":"21145","relation":"research_data"},{"status":"public","id":"22334","relation":"dissertation_contains"}],"link":[{"url":"https://ista.ac.at/en/news/how-proteins-breathe/","relation":"research_data","description":"News on ISTA website"}]},"pmid":1,"user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","author":[{"full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","last_name":"Becker","first_name":"Lea Marie"},{"last_name":"Fu","first_name":"Haohao","full_name":"Fu, Haohao"},{"last_name":"Tatman","first_name":"Benjamin","full_name":"Tatman, Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f"},{"full_name":"Dreydoppel, Matthias","first_name":"Matthias","last_name":"Dreydoppel"},{"last_name":"Kapitonova","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","full_name":"Kapitonova, Anna"},{"orcid":"0000-0001-7597-043X","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","full_name":"Balazs, Daniel","first_name":"Daniel","last_name":"Balazs"},{"first_name":"Ulrich","last_name":"Weininger","full_name":"Weininger, Ulrich"},{"full_name":"Engilberge, Sylvain","first_name":"Sylvain","last_name":"Engilberge"},{"first_name":"Christophe","last_name":"Chipot","full_name":"Chipot, Christophe"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"}],"OA_place":"publisher","volume":18,"title":"Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes","page":"1221-1230","license":"https://creativecommons.org/licenses/by/4.0/","article_processing_charge":"Yes (via OA deal)","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."}],"external_id":{"pmid":["42271006"]},"publication_status":"published"},{"day":"31","status":"public","doi":"10.15479/AT-ISTA-19696","tmp":{"short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"contributor":[{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","contributor_type":"project_leader","last_name":"Schanda"},{"first_name":"Vidhyalakshmi","contributor_type":"researcher","last_name":"Sridharan"},{"first_name":"Motilal","last_name":"Uttarkabat","contributor_type":"researcher"},{"last_name":"Jaroniec","contributor_type":"researcher","first_name":"Christopher"},{"contributor_type":"researcher","last_name":"Ernst","first_name":"Matthias"},{"orcid":"0000-0001-8729-7326","id":"c316e53f-b965-11eb-b128-bb26acc59c00","contributor_type":"researcher","last_name":"Rovo","first_name":"Petra"}],"year":"2025","date_created":"2025-05-14T10:46:07Z","has_accepted_license":"1","file":[{"date_updated":"2025-07-31T08:14:40Z","file_size":557878455,"checksum":"4c2d29404e070bda7d5619f728ec555c","relation":"main_file","access_level":"open_access","file_id":"20094","creator":"btatman","success":1,"content_type":"application/zip","file_name":"dataset.zip","date_created":"2025-07-31T08:14:40Z"},{"checksum":"6cbccd602be0ecb6ddb1f81fdfcadf92","relation":"main_file","access_level":"open_access","file_size":3514,"date_updated":"2025-07-31T08:14:21Z","file_id":"20095","creator":"btatman","success":1,"date_created":"2025-07-31T08:14:21Z","file_name":"readme.txt","content_type":"text/plain"}],"corr_author":"1","citation":{"apa":"Tatman, B. (2025). Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-19696\">https://doi.org/10.15479/AT-ISTA-19696</a>","chicago":"Tatman, Benjamin. “Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.’” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-19696\">https://doi.org/10.15479/AT-ISTA-19696</a>.","mla":"Tatman, Benjamin. <i>Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.”</i> Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19696\">10.15479/AT-ISTA-19696</a>.","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.","short":"B. Tatman, (2025).","ama":"Tatman B. Dataset for “Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State.” 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-19696\">10.15479/AT-ISTA-19696</a>","ista":"Tatman B. 2025. Dataset for ‘Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-19696\">10.15479/AT-ISTA-19696</a>."},"_id":"19696","related_material":{"link":[{"description":"Paper to which the dataset corresponds.","url":"http.//doi.org/10.1021/jacs.5c09057","relation":"research_paper"}],"record":[{"status":"public","id":"20321","relation":"research_data"}]},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"type":"research_data","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","oa_version":"Published Version","author":[{"first_name":"Benjamin","last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin"}],"publisher":"Institute of Science and Technology Austria","department":[{"_id":"PaSc"}],"date_updated":"2026-06-10T08:33:41Z","month":"07","title":"Dataset for \"Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State\"","date_published":"2025-07-31T00:00:00Z","oa":1,"file_date_updated":"2025-07-31T08:14:40Z","license":"https://creativecommons.org/licenses/by-nc-sa/4.0/","article_processing_charge":"No"},{"file":[{"date_created":"2025-09-10T07:53:10Z","content_type":"application/pdf","file_name":"2025_JACS_Tatman.pdf","success":1,"creator":"dernst","file_id":"20337","access_level":"open_access","relation":"main_file","checksum":"b350d56ddddefea96cebd62c277c0ff5","date_updated":"2025-09-10T07:53:10Z","file_size":5235353}],"quality_controlled":"1","corr_author":"1","ddc":["540"],"has_accepted_license":"1","date_created":"2025-09-10T05:37:19Z","year":"2025","publication":"Journal of the American Chemical Society","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"doi":"10.1021/jacs.5c09057","issue":"32","publication_status":"published","external_id":{"pmid":["40748291"],"isi":["001542746200001"]},"abstract":[{"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.","lang":"eng"}],"article_processing_charge":"Yes (via OA deal)","page":"29315-29326","title":"Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR","OA_place":"publisher","volume":147,"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","author":[{"first_name":"Benjamin","last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin"},{"first_name":"Vidhyalakshmi","last_name":"Sridharan","full_name":"Sridharan, Vidhyalakshmi"},{"full_name":"Uttarkabat, Motilal","last_name":"Uttarkabat","first_name":"Motilal"},{"full_name":"Jaroniec, Christopher P.","first_name":"Christopher P.","last_name":"Jaroniec"},{"last_name":"Ernst","first_name":"Matthias","full_name":"Ernst, Matthias"},{"last_name":"Rovo","first_name":"Petra","full_name":"Rovo, Petra","orcid":"0000-0001-8729-7326","id":"c316e53f-b965-11eb-b128-bb26acc59c00"},{"first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"}],"pmid":1,"related_material":{"record":[{"relation":"used_in_publication","id":"19696","status":"public"}]},"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"citation":{"chicago":"Tatman, Benjamin, Vidhyalakshmi Sridharan, Motilal Uttarkabat, Christopher P. Jaroniec, Matthias Ernst, Petra Rovo, and Paul Schanda. “Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2025. <a href=\"https://doi.org/10.1021/jacs.5c09057\">https://doi.org/10.1021/jacs.5c09057</a>.","apa":"Tatman, B., Sridharan, V., Uttarkabat, M., Jaroniec, C. P., Ernst, M., Rovo, P., &#38; Schanda, P. (2025). Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.5c09057\">https://doi.org/10.1021/jacs.5c09057</a>","mla":"Tatman, Benjamin, et al. “Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.” <i>Journal of the American Chemical Society</i>, vol. 147, no. 32, American Chemical Society, 2025, pp. 29315–26, doi:<a href=\"https://doi.org/10.1021/jacs.5c09057\">10.1021/jacs.5c09057</a>.","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.","ieee":"B. Tatman <i>et al.</i>, “Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR,” <i>Journal of the American Chemical Society</i>, vol. 147, no. 32. American Chemical Society, pp. 29315–29326, 2025.","ama":"Tatman B, Sridharan V, Uttarkabat M, et al. Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR. <i>Journal of the American Chemical Society</i>. 2025;147(32):29315-29326. doi:<a href=\"https://doi.org/10.1021/jacs.5c09057\">10.1021/jacs.5c09057</a>","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."},"PlanS_conform":"1","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"OA_type":"hybrid","day":"01","status":"public","file_date_updated":"2025-09-10T07:53:10Z","oa":1,"isi":1,"date_updated":"2026-06-10T08:33:41Z","publisher":"American Chemical Society","department":[{"_id":"PaSc"},{"_id":"NMR"}],"date_published":"2025-08-01T00:00:00Z","language":[{"iso":"eng"}],"month":"08","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.","type":"journal_article","oa_version":"Published Version","intvolume":"       147","article_type":"original","scopus_import":"1","_id":"20321"},{"PlanS_conform":"1","citation":{"chicago":"Rohden, Darja, Federico Napoli, Anna Kapitonova, Benjamin Tatman, Roman J. Lichtenecker, and Paul Schanda. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>.","apa":"Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &#38; Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>","mla":"Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169379, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>.","short":"D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda, Journal of Molecular Biology 437 (2025).","ieee":"D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R. J. Lichtenecker, and P. Schanda, “Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025.","ista":"Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. 2025. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. Journal of Molecular Biology. 437(23), 169379.","ama":"Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>"},"project":[{"grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery"}],"OA_type":"hybrid","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"status":"public","day":"01","isi":1,"oa":1,"file_date_updated":"2025-12-29T14:51:40Z","month":"12","language":[{"iso":"eng"}],"date_published":"2025-12-01T00:00:00Z","publisher":"Elsevier","department":[{"_id":"PaSc"}],"date_updated":"2026-08-13T14:19:01Z","article_type":"original","oa_version":"Published Version","intvolume":"       437","acknowledgement":"This work was supported financially by the Austrian Science Fund (FWF, Grant No. I5812-B, “AlloSpace”). This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility (LSF). We thank Petra Rovò and Margarita Valhondo Falcón for excellent support of the NMR facility.","type":"journal_article","_id":"20258","scopus_import":"1","corr_author":"1","file":[{"file_size":2270555,"date_updated":"2025-12-29T14:51:40Z","checksum":"90d50594d8ea9860ac5da41297992847","relation":"main_file","access_level":"open_access","file_id":"20876","creator":"dernst","success":1,"content_type":"application/pdf","file_name":"2025_JourMolecularBiology_Rohden.pdf","date_created":"2025-12-29T14:51:40Z"}],"quality_controlled":"1","has_accepted_license":"1","ddc":["540"],"year":"2025","date_created":"2025-08-31T22:01:33Z","article_number":"169379","issue":"23","doi":"10.1016/j.jmb.2025.169379","publication_identifier":{"eissn":["1089-8638"],"issn":["0022-2836"]},"publication":"Journal of Molecular Biology","article_processing_charge":"Yes (via OA deal)","abstract":[{"text":"The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise deuterated proteins holds great potential for high-resolution solution and magic-angle spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues play key roles for example at active sites of enzymes. Taking advantage of a chemically synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we demonstrate here the usefulness of proton-detected MAS NMR approaches to probe arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric enzyme malate dehydrogenase we detected a wide range of motions, from sites that are rigid on time scales of at least tens of milliseconds to residues undergoing predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled quantitative determination of these dynamics. We observed microsecond dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different β-turn conformations on this time scale. The labeling scheme and experiments presented here expand the toolkit for high-resolution proton-detected MAS NMR.","lang":"eng"}],"external_id":{"isi":["001618289100020"]},"publication_status":"published","title":"Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme","author":[{"last_name":"Rohden","first_name":"Darja","full_name":"Rohden, Darja","id":"81dc668a-19fa-11f0-bf31-d56534059ef3"},{"full_name":"Napoli, Federico","orcid":"0000-0002-9043-136X","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","first_name":"Federico","last_name":"Napoli"},{"last_name":"Kapitonova","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","full_name":"Kapitonova, Anna"},{"id":"71cda2f3-e604-11ee-a1df-da10587eda3f","full_name":"Tatman, Benjamin","last_name":"Tatman","first_name":"Benjamin"},{"full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker","first_name":"Roman J."},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":437,"OA_place":"publisher","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"related_material":{"record":[{"id":"19956","relation":"research_data","status":"public"}]}}]