[{"date_updated":"2026-06-10T09:28:41Z","file_date_updated":"2026-02-17T10:11:14Z","file":[{"date_created":"2026-02-17T10:11:14Z","file_id":"21285","creator":"lbecker","content_type":"application/zip","file_name":"Research_data.zip","relation":"main_file","success":1,"access_level":"open_access","date_updated":"2026-02-17T10:11:14Z","file_size":36996027,"checksum":"2d3105f26be578073b88ee1f2ea0bdb1"},{"content_type":"text/plain","file_id":"21286","creator":"lbecker","relation":"table_of_contents","file_name":"README.txt","date_created":"2026-02-17T10:11:14Z","checksum":"e24aebcdb8856cb181cbaa02de020ddb","file_size":1993,"date_updated":"2026-02-17T10:11:14Z","access_level":"open_access"}],"fulldoi":"https://doi.org/10.15479/AT-ISTA-21284","month":"2","year":"2026","publisher":"Institute of Science and Technology Austria","author":[{"full_name":"Becker, Lea Marie","last_name":"Becker","first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151"},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul"}],"abstract":[{"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.","lang":"eng"}],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"article_processing_charge":"No","doi":"10.15479/AT-ISTA-21284","has_accepted_license":"1","oa":1,"ddc":["541"],"_id":"21284","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.","license":"https://creativecommons.org/licenses/by-nc/4.0/","citation":{"ista":"Becker LM, Schanda P. 2026. Research data for ‘Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-21284\">10.15479/AT-ISTA-21284</a>.","ieee":"L. M. Becker and P. Schanda, “Research data for ‘Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.’” Institute of Science and Technology Austria, 2026.","apa":"Becker, L. M., &#38; Schanda, P. (2026). Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-21284\">https://doi.org/10.15479/AT-ISTA-21284</a>","short":"L.M. Becker, P. Schanda, (2026).","mla":"Becker, Lea Marie, and Paul Schanda. <i>Research Data for “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.”</i> Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21284\">10.15479/AT-ISTA-21284</a>.","chicago":"Becker, Lea Marie, and Paul Schanda. “Research Data for ‘Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.’” Institute of Science and Technology Austria, 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-21284\">https://doi.org/10.15479/AT-ISTA-21284</a>.","ama":"Becker LM, Schanda P. Research data for “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants.” 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21284\">10.15479/AT-ISTA-21284</a>"},"day":"18","date_created":"2026-02-17T10:17:14Z","corr_author":"1","tmp":{"short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"type":"research_data","contributor":[{"contributor_type":"researcher","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","first_name":"Giorgia","last_name":"Toscano"},{"contributor_type":"researcher","last_name":"Kapitonova","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471"},{"first_name":"Rajkumar","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20","last_name":"Singh","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Guillerm","id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","first_name":"Undina"},{"first_name":"Roman","last_name":"Lichtenecker","contributor_type":"researcher"}],"date_published":"2026-02-18T00:00:00Z","title":"Research data for \"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants\"","oa_version":"Published Version","status":"public","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","OA_place":"repository","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"OA_type":"free access"},{"date_updated":"2026-07-20T09:49:12Z","main_file_link":[{"url":"https://doi.org/10.5194/mr-7-29-2026","open_access":"1"}],"fulldoi":"https://doi.org/10.5194/mr-7-29-2026","pmid":1,"year":"2026","publisher":"Copernicus Publications","month":"04","volume":7,"article_processing_charge":"Yes","abstract":[{"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.","lang":"eng"}],"department":[{"_id":"PaSc"},{"_id":"GradSch"}],"doi":"10.5194/mr-7-29-2026","author":[{"last_name":"Becker","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie"},{"last_name":"Toscano","id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","first_name":"Giorgia","full_name":"Toscano, Giorgia"},{"last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna","full_name":"Kapitonova, Anna"},{"full_name":"Singh, Rajkumar","last_name":"Singh","first_name":"Rajkumar","id":"a3089acd-6806-11ee-bacc-f0c7d500ad20"},{"last_name":"Guillerm","id":"bb74f472-ae54-11eb-9835-bc9c22fb1183","first_name":"Undina","full_name":"Guillerm, Undina"},{"full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker","first_name":"Roman J."},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul"}],"page":"29-37","_id":"21777","issue":"1","ddc":["540"],"has_accepted_license":"1","intvolume":"         7","oa":1,"language":[{"iso":"eng"}],"external_id":{"pmid":["42057802"]},"citation":{"ieee":"L. M. Becker <i>et al.</i>, “Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants,” <i>Magnetic Resonance</i>, vol. 7, no. 1. Copernicus Publications, pp. 29–37, 2026.","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.","short":"L.M. Becker, G. Toscano, A. Kapitonova, R. Singh, U. Guillerm, R.J. Lichtenecker, P. Schanda, Magnetic Resonance 7 (2026) 29–37.","apa":"Becker, L. M., Toscano, G., Kapitonova, A., Singh, R., Guillerm, U., Lichtenecker, R. J., &#38; Schanda, P. (2026). Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>","chicago":"Becker, Lea Marie, Giorgia Toscano, Anna Kapitonova, Rajkumar Singh, Undina Guillerm, Roman J. Lichtenecker, and Paul Schanda. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>. Copernicus Publications, 2026. <a href=\"https://doi.org/10.5194/mr-7-29-2026\">https://doi.org/10.5194/mr-7-29-2026</a>.","mla":"Becker, Lea Marie, et al. “Accelerated 19F Biomolecular Magic-Angle Spinning NMR with Paramagnetic Dopants.” <i>Magnetic Resonance</i>, vol. 7, no. 1, Copernicus Publications, 2026, pp. 29–37, doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>.","ama":"Becker LM, Toscano G, Kapitonova A, et al. Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants. <i>Magnetic Resonance</i>. 2026;7(1):29-37. doi:<a href=\"https://doi.org/10.5194/mr-7-29-2026\">10.5194/mr-7-29-2026</a>"},"project":[{"_id":"B67AFEDC-15C9-11EA-A837-991A96BB2854","name":"IST Austria Open Access Fund"},{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777"}],"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).","related_material":{"record":[{"status":"public","id":"22334","relation":"dissertation_contains"}]},"DOAJ_listed":"1","license":"https://creativecommons.org/licenses/by/4.0/","type":"journal_article","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"day":"16","date_created":"2026-05-03T22:01:36Z","scopus_import":"1","article_type":"original","corr_author":"1","date_published":"2026-04-16T00:00:00Z","oa_version":"Published Version","title":"Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants","quality_controlled":"1","PlanS_conform":"1","publication_identifier":{"eissn":["2699-0016"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Magnetic Resonance","publication_status":"published","status":"public","OA_type":"gold","OA_place":"publisher","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}]},{"date_updated":"2026-08-04T09:32:45Z","file_date_updated":"2026-07-16T09:17:08Z","file":[{"date_created":"2026-07-16T09:17:08Z","content_type":"application/zip","file_id":"22346","creator":"lbecker","relation":"source_file","file_name":"2026_Becker_Lea_source_files.zip","access_level":"closed","date_updated":"2026-07-16T09:17:08Z","checksum":"8b85114eff543916c0e1445cd2189555","file_size":99472908},{"date_created":"2026-07-16T09:17:05Z","content_type":"application/pdf","creator":"lbecker","file_id":"22347","success":1,"relation":"main_file","file_name":"2026_Becker_Lea_Thesis.pdf","access_level":"open_access","date_updated":"2026-07-16T09:17:05Z","file_size":74647289,"checksum":"6c526862bc6dbd1e4c80ecb34580bc58"}],"alternative_title":["ISTA Thesis"],"fulldoi":"https://doi.org/10.15479/AT-ISTA-22334","month":"07","publisher":"Institute of Science and Technology Austria","doi_confirm":"1","year":"2026","supervisor":[{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul"}],"page":"205","author":[{"id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","orcid":"0000-0002-6401-5151","last_name":"Becker","full_name":"Becker, Lea Marie"}],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"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"}],"article_processing_charge":"No","doi":"10.15479/AT-ISTA-22334","has_accepted_license":"1","oa":1,"ddc":["572"],"language":[{"iso":"eng"}],"das_tickbox":"1","_id":"22334","related_material":{"record":[{"relation":"part_of_dissertation","id":"12675","status":"public"},{"status":"public","relation":"part_of_dissertation","id":"21777"},{"status":"public","relation":"part_of_dissertation","id":"12114"},{"id":"22105","relation":"part_of_dissertation","status":"public"}]},"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).","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","citation":{"chicago":"Becker, Lea Marie. “Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR.” Institute of Science and Technology Austria, 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-22334\">https://doi.org/10.15479/AT-ISTA-22334</a>.","mla":"Becker, Lea Marie. <i>Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR</i>. Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22334\">10.15479/AT-ISTA-22334</a>.","ama":"Becker LM. Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR. 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22334\">10.15479/AT-ISTA-22334</a>","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.","short":"L.M. Becker, Exploring Protein Dynamics Using Specific Labeling Approaches for Solid-State MAS NMR, Institute of Science and Technology Austria, 2026.","apa":"Becker, L. M. (2026). <i>Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-22334\">https://doi.org/10.15479/AT-ISTA-22334</a>"},"project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777"}],"day":"13","date_created":"2026-07-14T08:08:51Z","corr_author":"1","tmp":{"short":"CC BY-NC-ND (4.0)","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)"},"type":"dissertation","date_published":"2026-07-13T00:00:00Z","title":"Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR","oa_version":"Published Version","degree_awarded":"PhD","status":"public","publication_status":"published","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"NMR"}],"OA_place":"publisher","publication_identifier":{"isbn":["978-3-99078-084-8"],"issn":["2663-337X"]}},{"date_created":"2026-06-21T22:03:01Z","scopus_import":"1","day":"01","article_type":"original","corr_author":"1","type":"journal_article","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"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).","related_material":{"link":[{"url":"https://ista.ac.at/en/news/how-proteins-breathe/","relation":"research_data","description":"News on ISTA website"}],"record":[{"id":"20641","relation":"research_data","status":"public"},{"status":"public","id":"21145","relation":"research_data"},{"relation":"dissertation_contains","id":"22334","status":"public"}]},"citation":{"apa":"Becker, L. M., Fu, H., Tatman, B., Dreydoppel, M., Kapitonova, A., Balazs, D., … Schanda, P. (2026). Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>","short":"L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U. Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry 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.","ieee":"L. M. Becker <i>et al.</i>, “Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes,” <i>Nature Chemistry</i>, vol. 18. Springer Nature, pp. 1221–1230, 2026.","ama":"Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. 2026;18:1221-1230. doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>","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>.","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>."},"project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777"}],"publication_status":"published","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","publication":"Nature Chemistry","status":"public","OA_place":"publisher","OA_type":"hybrid","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"publication_identifier":{"eissn":["17554349"],"issn":["17554330"]},"quality_controlled":"1","PlanS_conform":"1","date_published":"2026-07-01T00:00:00Z","title":"Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes","oa_version":"Published Version","supplementarymaterial":"yes","fulldoi":"https://doi.org/10.1038/s41557-026-02155-0","pmid":1,"publisher":"Springer Nature","year":"2026","month":"07","volume":18,"date_updated":"2026-08-04T09:32:45Z","file_date_updated":"2026-07-28T06:58:35Z","file":[{"file_size":2618184,"checksum":"1069fb27949fd2cb641b043b3a96a580","access_level":"open_access","date_updated":"2026-07-28T06:58:35Z","creator":"dernst","file_id":"22595","content_type":"application/pdf","relation":"main_file","file_name":"2026_NatureChemistry_Becker.pdf","success":1,"date_created":"2026-07-28T06:58:35Z"}],"ddc":["540"],"oa":1,"has_accepted_license":"1","intvolume":"        18","language":[{"iso":"eng"}],"das_tickbox":"1","external_id":{"pmid":["42271006"]},"_id":"22105","author":[{"last_name":"Becker","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","first_name":"Lea Marie","full_name":"Becker, Lea Marie"},{"last_name":"Fu","first_name":"Haohao","full_name":"Fu, Haohao"},{"last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin","full_name":"Tatman, Benjamin"},{"full_name":"Dreydoppel, Matthias","first_name":"Matthias","last_name":"Dreydoppel"},{"id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna","last_name":"Kapitonova","full_name":"Kapitonova, Anna"},{"full_name":"Balazs, Daniel","last_name":"Balazs","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","orcid":"0000-0001-7597-043X","first_name":"Daniel"},{"first_name":"Ulrich","last_name":"Weininger","full_name":"Weininger, Ulrich"},{"last_name":"Engilberge","first_name":"Sylvain","full_name":"Engilberge, Sylvain"},{"full_name":"Chipot, Christophe","first_name":"Christophe","last_name":"Chipot"},{"full_name":"Schanda, Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606"}],"page":"1221-1230","article_processing_charge":"Yes (via OA deal)","researchdata_availability":"yes","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."}],"department":[{"_id":"PaSc"},{"_id":"LifeSc"}],"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.","doi":"10.1038/s41557-026-02155-0"},{"_id":"21145","oa":1,"has_accepted_license":"1","ddc":["572"],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"abstract":[{"text":"Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. ","lang":"eng"}],"article_processing_charge":"No","doi":"10.15479/AT-ISTA-21145","author":[{"last_name":"Becker","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","full_name":"Becker, Lea Marie"},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul"},{"full_name":"Chipot, Christophe","last_name":"Chipot","first_name":"Christophe"}],"fulldoi":"https://doi.org/10.15479/AT-ISTA-21145","year":"2026","publisher":"Institute of Science and Technology Austria","month":"02","file_date_updated":"2026-02-05T13:52:41Z","file":[{"date_created":"2026-02-05T13:52:37Z","relation":"table_of_contents","file_name":"README.txt","content_type":"text/plain","creator":"lbecker","file_id":"21146","access_level":"open_access","date_updated":"2026-02-05T13:52:37Z","checksum":"02a419cce8cea450bc952f35488d2df5","file_size":4263},{"success":1,"file_name":"Research_Data.zip","relation":"main_file","content_type":"application/zip","file_id":"21147","creator":"lbecker","date_created":"2026-02-05T13:52:41Z","checksum":"b0b82b1aa73985b0b308a3fa52d21aea","file_size":50647107,"date_updated":"2026-02-05T13:52:41Z","access_level":"open_access"}],"date_updated":"2026-08-04T09:32:45Z","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"date_published":"2026-02-09T00:00:00Z","oa_version":"Published Version","title":"Additional Data for \"Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes\"","contributor":[{"last_name":"Fu","first_name":"Haohao","contributor_type":"researcher"},{"last_name":"Tatman","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Dreydoppel","first_name":"Matthias"},{"contributor_type":"researcher","last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna"},{"last_name":"Balazs","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","first_name":"Daniel","orcid":"0000-0001-7597-043X","contributor_type":"researcher"},{"contributor_type":"researcher","first_name":"Ulrich","last_name":"Weininger"},{"last_name":"Engilberge","first_name":"Sylvain","contributor_type":"researcher"}],"tmp":{"short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"type":"research_data","date_created":"2026-02-05T13:54:39Z","day":"09","corr_author":"1","citation":{"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, <a href=\"https://doi.org/10.15479/AT-ISTA-21145\">10.15479/AT-ISTA-21145</a>.","short":"L.M. Becker, P. Schanda, C. Chipot, (2026).","apa":"Becker, L. M., Schanda, P., &#38; Chipot, C. (2026). Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-21145\">https://doi.org/10.15479/AT-ISTA-21145</a>","chicago":"Becker, Lea Marie, Paul Schanda, and Christophe Chipot. “Additional Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-21145\">https://doi.org/10.15479/AT-ISTA-21145</a>.","mla":"Becker, Lea Marie, et al. <i>Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.”</i> Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21145\">10.15479/AT-ISTA-21145</a>.","ama":"Becker LM, Schanda P, Chipot C. Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21145\">10.15479/AT-ISTA-21145</a>"},"project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777"}],"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.","related_material":{"record":[{"id":"20641","relation":"earlier_version","status":"public"},{"id":"22105","relation":"used_in_publication","status":"public"}]}},{"title":"Data for \"Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes\"","oa_version":"Published Version","date_published":"2025-11-18T00:00:00Z","contributor":[{"last_name":"Fu","first_name":"Haohao ","contributor_type":"researcher"},{"first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman","contributor_type":"researcher"},{"contributor_type":"researcher","first_name":"Matthias","last_name":"Dreydoppel"},{"last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","first_name":"Anna","contributor_type":"researcher"},{"last_name":"Balazs","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","first_name":"Daniel","orcid":"0000-0001-7597-043X","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Weininger","first_name":"Ulrich"},{"last_name":"Engilberge","first_name":"Sylvain","contributor_type":"researcher"},{"last_name":"Chipot","first_name":"Christophe","contributor_type":"researcher"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"status":"public","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","project":[{"_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches"}],"citation":{"apa":"Becker, L. M., &#38; Schanda, P. (2025). Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-20641\">https://doi.org/10.15479/AT-ISTA-20641</a>","short":"L.M. Becker, P. Schanda, (2025).","ista":"Becker LM, Schanda P. 2025. Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes’, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT-ISTA-20641\">10.15479/AT-ISTA-20641</a>.","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.","ama":"Becker LM, Schanda P. Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20641\">10.15479/AT-ISTA-20641</a>","mla":"Becker, Lea Marie, and Paul Schanda. <i>Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.”</i> Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20641\">10.15479/AT-ISTA-20641</a>.","chicago":"Becker, Lea Marie, and Paul Schanda. “Data for ‘Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.’” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-20641\">https://doi.org/10.15479/AT-ISTA-20641</a>."},"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.","related_material":{"record":[{"status":"public","id":"21145","relation":"later_version"},{"relation":"used_in_publication","id":"22105","status":"public"}]},"tmp":{"short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"type":"research_data","corr_author":"1","day":"18","date_created":"2025-11-13T09:29:58Z","doi":"10.15479/AT-ISTA-20641","abstract":[{"text":"Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. ","lang":"eng"}],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"article_processing_charge":"No","author":[{"full_name":"Becker, Lea Marie","first_name":"Lea Marie","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","last_name":"Becker"},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda"}],"_id":"20641","has_accepted_license":"1","oa":1,"ddc":["572"],"file":[{"checksum":"a73a0550c644957e7f62241e239d3a1d","file_size":1806589513,"date_updated":"2026-02-17T10:16:57Z","access_level":"open_access","content_type":"application/zip","file_id":"20643","creator":"lbecker","file_name":"Research_Data.zip","relation":"main_file","date_created":"2025-11-13T09:38:35Z"},{"date_created":"2025-11-17T11:54:17Z","relation":"table_of_contents","file_name":"README.pdf","content_type":"application/pdf","file_id":"20652","creator":"lbecker","date_updated":"2026-02-17T10:16:57Z","access_level":"open_access","checksum":"7176b257f753c213a0460ee06f802363","file_size":191376}],"file_date_updated":"2026-02-17T10:16:57Z","date_updated":"2026-08-04T09:32:44Z","year":"2025","publisher":"Institute of Science and Technology Austria","month":"11","fulldoi":"https://doi.org/10.15479/AT-ISTA-20641"},{"department":[{"_id":"PaSc"}],"abstract":[{"text":"Dynamic processes in molecules can occur on a wide range of timescales, and it is important to understand which timescales of motion contribute to different parameters used in dynamics measurements. For spin relaxation, this can easily be understood from the sampling frequencies of the spectral-density function by different relaxation-rate constants. In addition to data from relaxation measurements, determining dynamically averaged anisotropic interactions in magic-angle spinning (MAS) solid-state NMR allows for better quantification of the amplitude of molecular motion. For partially averaged anisotropic interactions, the relevant timescales of motion are not so clearly defined. Whether the averaging depends on the experimental methods (e.g., pulse sequences) or conditions (e.g., MAS frequency, magnitude of anisotropic interaction, radio-frequency field amplitudes) is not fully understood. To investigate these questions, we performed numerical simulations of dynamic systems based on the stochastic Liouville equation using several experiments for recoupling the dipolar coupling, chemical-shift anisotropy or quadrupolar coupling. As described in the literature, the transition between slow motion, where parameters characterizing the anisotropic interaction are not averaged, and fast motion, where the tensors are averaged leading to a scaled anisotropic quantity, occurs over a window of motional rate constants that depends mainly on the strength of the interaction. This transition region can span 2 orders of magnitude in exchange-rate constants (typically in the microsecond range) but depends only marginally on the employed recoupling scheme or sample spinning frequency. The transition region often coincides with a fast relaxation of coherences, making precise quantitative measurements difficult. Residual couplings in off-magic-angle experiments, however, average over longer timescales of motion. While in principle one may gain information on the timescales of motion from the transition area, extracting such information is hampered by low signal-to-noise ratio in experimental spectra due to fast relaxation that occurs in the same region.","lang":"eng"}],"article_processing_charge":"Yes","doi":"10.5194/mr-5-69-2024","page":"69-86","author":[{"first_name":"Kathrin","last_name":"Aebischer","full_name":"Aebischer, Kathrin"},{"last_name":"Becker","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","first_name":"Lea Marie","full_name":"Becker, Lea Marie"},{"last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"full_name":"Ernst, Matthias","last_name":"Ernst","first_name":"Matthias"}],"_id":"17161","issue":"1","intvolume":"         5","oa":1,"has_accepted_license":"1","ddc":["530"],"external_id":{"pmid":["40384772"]},"language":[{"iso":"eng"}],"file_date_updated":"2024-06-27T06:42:55Z","file":[{"file_size":6736194,"checksum":"d01074f6919387fcaf8c9ebed320ccae","access_level":"open_access","date_updated":"2024-06-27T06:42:55Z","creator":"dernst","file_id":"17181","content_type":"application/pdf","file_name":"2024_MagneticResonance_Aebischer.pdf","relation":"main_file","success":1,"date_created":"2024-06-27T06:42:55Z"}],"date_updated":"2026-09-11T08:49:55Z","pmid":1,"fulldoi":"https://doi.org/10.5194/mr-5-69-2024","volume":5,"year":"2024","publisher":"Copernicus Publications","month":"06","date_published":"2024-06-11T00:00:00Z","title":"Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR","oa_version":"Published Version","quality_controlled":"1","publication_identifier":{"eissn":["2699-0016"]},"status":"public","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Magnetic Resonance","citation":{"ista":"Aebischer K, Becker LM, Schanda P, Ernst M. 2024. Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. Magnetic Resonance. 5(1), 69–86.","ieee":"K. Aebischer, L. M. Becker, P. Schanda, and M. Ernst, “Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR,” <i>Magnetic Resonance</i>, vol. 5, no. 1. Copernicus Publications, pp. 69–86, 2024.","apa":"Aebischer, K., Becker, L. M., Schanda, P., &#38; Ernst, M. (2024). Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. <i>Magnetic Resonance</i>. Copernicus Publications. <a href=\"https://doi.org/10.5194/mr-5-69-2024\">https://doi.org/10.5194/mr-5-69-2024</a>","short":"K. Aebischer, L.M. Becker, P. Schanda, M. Ernst, Magnetic Resonance 5 (2024) 69–86.","mla":"Aebischer, Kathrin, et al. “Evaluating the Motional Timescales Contributing to Averaged Anisotropic Interactions in MAS Solid-State NMR.” <i>Magnetic Resonance</i>, vol. 5, no. 1, Copernicus Publications, 2024, pp. 69–86, doi:<a href=\"https://doi.org/10.5194/mr-5-69-2024\">10.5194/mr-5-69-2024</a>.","chicago":"Aebischer, Kathrin, Lea Marie Becker, Paul Schanda, and Matthias Ernst. “Evaluating the Motional Timescales Contributing to Averaged Anisotropic Interactions in MAS Solid-State NMR.” <i>Magnetic Resonance</i>. Copernicus Publications, 2024. <a href=\"https://doi.org/10.5194/mr-5-69-2024\">https://doi.org/10.5194/mr-5-69-2024</a>.","ama":"Aebischer K, Becker LM, Schanda P, Ernst M. Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR. <i>Magnetic Resonance</i>. 2024;5(1):69-86. doi:<a href=\"https://doi.org/10.5194/mr-5-69-2024\">10.5194/mr-5-69-2024</a>"},"project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","grant_number":"26777","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0"}],"related_material":{"record":[{"status":"public","relation":"research_data","id":"22906"}]},"acknowledgement":"We would like to thank Kay Saalwächter for pointing out important aspects of the intermediate regime during the open review process. Lea Marie Becker is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria.\r\nThis research has been supported by the Österreichischen Akademie der Wissenschaften (grant no. PR10660EAW01) and the Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (grant nos. 200020_188988 and 200020_219375).","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"type":"journal_article","article_type":"original","scopus_import":"1","day":"11","date_created":"2024-06-23T22:01:02Z"},{"has_accepted_license":"1","status":"public","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","ddc":["572"],"_id":"12497","contributor":[{"contributor_type":"researcher","last_name":"Berbon","first_name":"Mélanie"},{"contributor_type":"researcher","last_name":"Vallet","first_name":"Alicia"},{"contributor_type":"researcher","last_name":"Grelard","first_name":"Axelle"},{"first_name":"Estelle","last_name":"Morvan","contributor_type":"researcher"},{"first_name":"Benjamin","last_name":"Bardiaux","contributor_type":"researcher"},{"contributor_type":"researcher","first_name":"Roman","last_name":"Lichtenecker"},{"contributor_type":"researcher","last_name":"Ernst","first_name":"Matthias"},{"contributor_type":"researcher","last_name":"Loquet","first_name":"Antoine"},{"contributor_type":"contact_person","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"contributor_type":"researcher","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","first_name":"Lea Marie","last_name":"Becker"}],"author":[{"full_name":"Becker, Lea Marie","last_name":"Becker","first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","full_name":"Schanda, Paul"}],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"abstract":[{"text":"Aromatic side chains are important reporters of the plasticity of proteins, and often form important contacts in protein–protein interactions. We studied aromatic residues in the two structurally homologous cross-β amyloid fibrils HET-s, and  HELLF by employing a specific isotope-labeling approach and magic-angle-spinning NMR. The dynamic behavior of the aromatic residues Phe and Tyr indicates that the hydrophobic amyloid core is rigid, without any sign of \"breathing motions\" over hundreds of milliseconds at least. Aromatic residues exposed at the fibril surface have a rigid ring axis but undergo ring flips on a variety of time scales from nanoseconds to microseconds. Our approach provides direct insight into hydrophobic-core motions, enabling a better evaluation of the conformational heterogeneity generated from an NMR structural ensemble of such amyloid cross-β architecture.","lang":"eng"}],"date_published":"2023-03-23T00:00:00Z","article_processing_charge":"No","doi":"10.15479/AT:ISTA:12497","title":"Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues","oa_version":"Published Version","keyword":["aromatic side chains","isotopic labeling","protein dynamics","ring flips","spin relaxation"],"date_created":"2023-02-03T08:08:02Z","fulldoi":"https://doi.org/10.15479/AT:ISTA:12497","day":"23","corr_author":"1","year":"2023","month":"03","publisher":"Institute of Science and Technology Austria","tmp":{"short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"type":"research_data","related_material":{"record":[{"status":"public","relation":"used_in_publication","id":"12675"}]},"date_updated":"2024-10-21T06:01:38Z","citation":{"ieee":"L. M. Becker and P. Schanda, “Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues.” Institute of Science and Technology Austria, 2023.","ista":"Becker LM, Schanda P. 2023. Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT:ISTA:12497\">10.15479/AT:ISTA:12497</a>.","short":"L.M. Becker, P. Schanda, (2023).","apa":"Becker, L. M., &#38; Schanda, P. (2023). Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:12497\">https://doi.org/10.15479/AT:ISTA:12497</a>","chicago":"Becker, Lea Marie, and Paul Schanda. “Research Data to: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy of Aromatic Residues.” Institute of Science and Technology Austria, 2023. <a href=\"https://doi.org/10.15479/AT:ISTA:12497\">https://doi.org/10.15479/AT:ISTA:12497</a>.","mla":"Becker, Lea Marie, and Paul Schanda. <i>Research Data to: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy of Aromatic Residues</i>. Institute of Science and Technology Austria, 2023, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:12497\">10.15479/AT:ISTA:12497</a>.","ama":"Becker LM, Schanda P. Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. 2023. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:12497\">10.15479/AT:ISTA:12497</a>"},"file_date_updated":"2023-03-24T09:42:03Z","file":[{"date_created":"2023-03-23T10:03:16Z","relation":"main_file","file_name":"Research_Data.zip","content_type":"application/zip","file_id":"12743","creator":"lbecker","access_level":"open_access","date_updated":"2023-03-24T09:34:20Z","file_size":87018103,"checksum":"fd9a28620a81a82991fb70f4fd6591d9"},{"file_name":"README.txt","relation":"main_file","content_type":"text/plain","file_id":"12755","creator":"dernst","date_created":"2023-03-24T07:13:55Z","file_size":747,"checksum":"30ebdfb600af118fcf8518b6efe0b7e9","access_level":"open_access","date_updated":"2023-03-24T09:42:03Z"}]},{"acknowledgement":"Wir danken Albert A. Smith (Leipzig) für aufschlussreiche Diskussionen. Diese Arbeit wurde mit Mitteln des Europäischen Forschungsrats (StG-2012-311318 an P.S.) unterstützt und nutzte die Plattformen des Grenoble Instruct-ERIC Center (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) im Rahmen der Grenoble Partnership for Structural Biology (PSB) sowie die Einrichtungen und das Fachwissen der Biophysical and Structural Chemistry Platform (BPCS) am IECB, CNRS UAR3033, INSERM US001 und der Universität Bordeaux.","citation":{"chicago":"Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.” <i>Angewandte Chemie</i>. Wiley, 2023. <a href=\"https://doi.org/10.1002/ange.202219314\">https://doi.org/10.1002/ange.202219314</a>.","mla":"Becker, Lea Marie, et al. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.” <i>Angewandte Chemie</i>, vol. 135, no. 19, e202219314, Wiley, 2023, doi:<a href=\"https://doi.org/10.1002/ange.202219314\">10.1002/ange.202219314</a>.","ama":"Becker LM, Berbon M, Vallet A, et al. Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. <i>Angewandte Chemie</i>. 2023;135(19). doi:<a href=\"https://doi.org/10.1002/ange.202219314\">10.1002/ange.202219314</a>","ieee":"L. M. Becker <i>et al.</i>, “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten,” <i>Angewandte Chemie</i>, vol. 135, no. 19. Wiley, 2023.","ista":"Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker R, Ernst M, Loquet A, Schanda P. 2023. Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte Chemie. 135(19), e202219314.","short":"L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie 135 (2023).","apa":"Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. <i>Angewandte Chemie</i>. Wiley. <a href=\"https://doi.org/10.1002/ange.202219314\">https://doi.org/10.1002/ange.202219314</a>"},"date_created":"2024-01-18T10:01:01Z","day":"02","article_type":"original","corr_author":"1","type":"journal_article","tmp":{"short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"quality_controlled":"1","date_published":"2023-05-02T00:00:00Z","oa_version":"Published Version","article_number":"e202219314","title":"Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten","publication_status":"published","publication":"Angewandte Chemie","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","publication_identifier":{"eissn":["1521-3757"],"issn":["0044-8249"]},"date_updated":"2024-10-09T21:07:55Z","file_date_updated":"2024-01-23T08:57:01Z","file":[{"content_type":"application/pdf","creator":"dernst","file_id":"14876","success":1,"relation":"main_file","file_name":"2023_AngewChem_Becker.pdf","date_created":"2024-01-23T08:57:01Z","checksum":"98e68d370159f7be52a3d7c8a8ee1198","file_size":1004676,"access_level":"open_access","date_updated":"2024-01-23T08:57:01Z"}],"fulldoi":"https://doi.org/10.1002/ange.202219314","keyword":["General Medicine"],"month":"05","year":"2023","publisher":"Wiley","volume":135,"author":[{"full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","first_name":"Lea Marie","last_name":"Becker"},{"last_name":"Berbon","first_name":"Mélanie","full_name":"Berbon, Mélanie"},{"first_name":"Alicia","last_name":"Vallet","full_name":"Vallet, Alicia"},{"full_name":"Grelard, Axelle","first_name":"Axelle","last_name":"Grelard"},{"full_name":"Morvan, Estelle","last_name":"Morvan","first_name":"Estelle"},{"last_name":"Bardiaux","first_name":"Benjamin","full_name":"Bardiaux, Benjamin"},{"first_name":"Roman","last_name":"Lichtenecker","full_name":"Lichtenecker, Roman"},{"full_name":"Ernst, Matthias","first_name":"Matthias","last_name":"Ernst"},{"full_name":"Loquet, Antoine","first_name":"Antoine","last_name":"Loquet"},{"full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"article_processing_charge":"Yes (in subscription journal)","department":[{"_id":"PaSc"}],"abstract":[{"lang":"ger","text":"Aromatische Seitenketten sind wichtige Indikatoren für die Plastizität von Proteinen und bilden oft entscheidende Kontakte bei Protein‐Protein‐Wechselwirkungen. Wir untersuchten aromatische Reste in den beiden strukturell homologen cross‐β Amyloidfibrillen HET‐s und HELLF mit Hilfe eines spezifischen Ansatzes zur Isotopenmarkierung und Festkörper NMR mit Drehung am magischen Winkel. Das dynamische Verhalten der aromatischen Reste Phe und Tyr deutet darauf hin, dass der hydrophobe Amyloidkern starr ist und keine Anzeichen von “atmenden Bewegungen” auf einer Zeitskala von Hunderten von Millisekunden zeigt. Aromatische Reste, die exponiert an der Fibrillenoberfläche sitzen, haben zwar eine starre Ringachse, weisen aber Ringflips auf verschiedenen Zeitskalen von Nanosekunden bis Mikrosekunden auf. Unser Ansatz bietet einen direkten Einblick in die Bewegungen des hydrophoben Kerns und ermöglicht eine bessere Bewertung der Konformationsheterogenität, die aus einem NMR‐Strukturensemble einer solchen Cross‐β‐Amyloidstruktur hervorgeht."}],"doi":"10.1002/ange.202219314","ddc":["540"],"oa":1,"intvolume":"       135","has_accepted_license":"1","language":[{"iso":"ger"}],"issue":"19","_id":"14835"},{"_id":"14861","issue":"19","ddc":["540"],"oa":1,"intvolume":"        62","language":[{"iso":"eng"}],"article_processing_charge":"No","department":[{"_id":"PaSc"}],"abstract":[{"lang":"eng","text":"Cover Page"}],"doi":"10.1002/anie.202304138","author":[{"orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","last_name":"Becker","full_name":"Becker, Lea Marie"},{"full_name":"Berbon, Mélanie","first_name":"Mélanie","last_name":"Berbon"},{"full_name":"Vallet, Alicia","last_name":"Vallet","first_name":"Alicia"},{"last_name":"Grelard","first_name":"Axelle","full_name":"Grelard, Axelle"},{"full_name":"Morvan, Estelle","last_name":"Morvan","first_name":"Estelle"},{"last_name":"Bardiaux","first_name":"Benjamin","full_name":"Bardiaux, Benjamin"},{"full_name":"Lichtenecker, Roman","first_name":"Roman","last_name":"Lichtenecker"},{"last_name":"Ernst","first_name":"Matthias","full_name":"Ernst, Matthias"},{"first_name":"Antoine","last_name":"Loquet","full_name":"Loquet, Antoine"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1002/anie.202304138"}],"fulldoi":"https://doi.org/10.1002/anie.202304138","keyword":["General Chemistry","Catalysis"],"year":"2023","month":"05","publisher":"Wiley","volume":62,"date_updated":"2026-06-18T17:41:09Z","publication_identifier":{"eissn":["1521-3773"],"issn":["1433-7851"]},"publication":"Angewandte Chemie International Edition","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","date_published":"2023-05-02T00:00:00Z","article_number":" e202304138","title":"Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues","oa_version":"Published Version","type":"other_academic_publication","day":"02","date_created":"2024-01-22T11:54:34Z","corr_author":"1","citation":{"ista":"Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker R, Ernst M, Loquet A, Schanda P. 2023. Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues, Wiley,p.","ieee":"L. M. Becker <i>et al.</i>, <i>Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues</i>, vol. 62, no. 19. Wiley, 2023.","apa":"Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). <i>Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues</i>. <i>Angewandte Chemie International Edition</i> (Vol. 62). Wiley. <a href=\"https://doi.org/10.1002/anie.202304138\">https://doi.org/10.1002/anie.202304138</a>","short":"L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues, Wiley, 2023.","mla":"Becker, Lea Marie, et al. “Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues.” <i>Angewandte Chemie International Edition</i>, vol. 62, no. 19, e202304138, Wiley, 2023, doi:<a href=\"https://doi.org/10.1002/anie.202304138\">10.1002/anie.202304138</a>.","chicago":"Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. <i>Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues</i>. <i>Angewandte Chemie International Edition</i>. Vol. 62. Wiley, 2023. <a href=\"https://doi.org/10.1002/anie.202304138\">https://doi.org/10.1002/anie.202304138</a>.","ama":"Becker LM, Berbon M, Vallet A, et al. <i>Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues</i>. Vol 62. Wiley; 2023. doi:<a href=\"https://doi.org/10.1002/anie.202304138\">10.1002/anie.202304138</a>"},"related_material":{"record":[{"id":"12675","relation":"other","status":"public"}],"link":[{"url":"https://doi.org/10.1002/ange.202304138","relation":"translation"}]}},{"doi":"10.1002/anie.202219314","article_processing_charge":"Yes (via OA deal)","abstract":[{"lang":"eng","text":"Aromatic side chains are important reporters of the plasticity of proteins, and often form important contacts in protein--protein interactions. By studying a pair of structurally homologous cross-β amyloid fibrils, HET-s and HELLF, with a specific isotope-labeling approach and magic-angle-spinning (MAS) NMR, we have characterized the dynamic behavior of Phe and Tyr aromatic rings to show that the hydrophobic amyloid core is rigid, without any sign of \"breathing motions\" over hundreds of milliseconds at least. Aromatic residues exposed at the fibril surface have a rigid ring axis but undergo ring flips, on a variety of time scales from ns to µs. Our approach provides direct insight into hydrophobic-core motions, enabling a better evaluation of the conformational heterogeneity generated from a NMR structural ensemble of such amyloid cross-β architecture."}],"department":[{"_id":"GradSch"},{"_id":"PaSc"}],"author":[{"orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","last_name":"Becker","full_name":"Becker, Lea Marie"},{"full_name":"Berbon, Mélanie","last_name":"Berbon","first_name":"Mélanie"},{"full_name":"Vallet, Alicia","first_name":"Alicia","last_name":"Vallet"},{"first_name":"Axelle","last_name":"Grelard","full_name":"Grelard, Axelle"},{"last_name":"Morvan","first_name":"Estelle","full_name":"Morvan, Estelle"},{"last_name":"Bardiaux","first_name":"Benjamin","full_name":"Bardiaux, Benjamin"},{"last_name":"Lichtenecker","first_name":"Roman","full_name":"Lichtenecker, Roman"},{"first_name":"Matthias","last_name":"Ernst","full_name":"Ernst, Matthias"},{"last_name":"Loquet","first_name":"Antoine","full_name":"Loquet, Antoine"},{"full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda"}],"issue":"19","_id":"12675","language":[{"iso":"eng"}],"external_id":{"isi":["000956919900001"],"pmid":["36738230"]},"ddc":["540"],"intvolume":"        62","has_accepted_license":"1","oa":1,"file":[{"success":1,"file_name":"2023_AngewChemInt_Becker.pdf","relation":"main_file","content_type":"application/pdf","file_id":"14072","creator":"dernst","date_created":"2023-08-16T12:33:31Z","file_size":1422445,"checksum":"7dd083ed8850faa55c34e411ed390de9","access_level":"open_access","date_updated":"2023-08-16T12:33:31Z"}],"file_date_updated":"2023-08-16T12:33:31Z","date_updated":"2026-07-20T09:49:12Z","year":"2023","publisher":"Wiley","month":"05","volume":62,"fulldoi":"https://doi.org/10.1002/anie.202219314","pmid":1,"keyword":["General Chemistry","Catalysis"],"title":"The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues","oa_version":"Published Version","article_number":"e202219314","date_published":"2023-05-01T00:00:00Z","quality_controlled":"1","publication_identifier":{"issn":["1433-7851"],"eissn":["1521-3773"]},"publication":"Angewandte Chemie International Edition","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","citation":{"ama":"Becker LM, Berbon M, Vallet A, et al. The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. <i>Angewandte Chemie International Edition</i>. 2023;62(19). doi:<a href=\"https://doi.org/10.1002/anie.202219314\">10.1002/anie.202219314</a>","mla":"Becker, Lea Marie, et al. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle Spinning NMR of Aromatic Residues.” <i>Angewandte Chemie International Edition</i>, vol. 62, no. 19, e202219314, Wiley, 2023, doi:<a href=\"https://doi.org/10.1002/anie.202219314\">10.1002/anie.202219314</a>.","chicago":"Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle Spinning NMR of Aromatic Residues.” <i>Angewandte Chemie International Edition</i>. Wiley, 2023. <a href=\"https://doi.org/10.1002/anie.202219314\">https://doi.org/10.1002/anie.202219314</a>.","apa":"Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. <i>Angewandte Chemie International Edition</i>. Wiley. <a href=\"https://doi.org/10.1002/anie.202219314\">https://doi.org/10.1002/anie.202219314</a>","short":"L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie International Edition 62 (2023).","ista":"Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker R, Ernst M, Loquet A, Schanda P. 2023. The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International Edition. 62(19), e202219314.","ieee":"L. M. Becker <i>et al.</i>, “The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues,” <i>Angewandte Chemie International Edition</i>, vol. 62, no. 19. Wiley, 2023."},"related_material":{"record":[{"status":"public","id":"12497","relation":"research_data"},{"relation":"other","id":"14861","status":"public"},{"relation":"dissertation_contains","id":"22334","status":"public"}],"link":[{"url":"https://ista.ac.at/en/news/dancing-styles-of-atoms/","relation":"press_release","description":"News on ISTA website"}]},"acknowledgement":"We thank AlbertA. Smith (Leipzig)for insightful discussions. This work was supported by funding from the European Research Council (StG-2012-311318 to P.S.) and used the platforms of the Grenoble Instruct-ERIC center (ISBG;UMS 3518 CNRS-CEA-UJF-EMBL) within the Grenoble Partnership for Structural Biology(PSB) and facilities and expertiseof the Biophysical and Structural Chemistry platform (BPCS) at IECB,CNRSUAR3033,INSERMUS001 and Bordeaux University.","type":"journal_article","tmp":{"short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"isi":1,"corr_author":"1","day":"01","scopus_import":"1","date_created":"2023-02-24T10:45:01Z","article_type":"original"},{"author":[{"first_name":"Diego F.","last_name":"Gauto","full_name":"Gauto, Diego F."},{"first_name":"Olga O.","last_name":"Lebedenko","full_name":"Lebedenko, Olga O."},{"last_name":"Becker","first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie"},{"last_name":"Ayala","first_name":"Isabel","full_name":"Ayala, Isabel"},{"last_name":"Lichtenecker","first_name":"Roman","full_name":"Lichtenecker, Roman"},{"full_name":"Skrynnikov, Nikolai R.","last_name":"Skrynnikov","first_name":"Nikolai R."},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"abstract":[{"lang":"eng","text":"Probing the dynamics of aromatic side chains provides important insights into the behavior of a protein because flips of aromatic rings in a protein’s hydrophobic core report on breathing motion involving a large part of the protein. Inherently invisible to crystallography, aromatic motions have been primarily studied by solution NMR. The question how packing of proteins in crystals affects ring flips has, thus, remained largely unexplored. Here we apply magic-angle spinning NMR, advanced phenylalanine 1H-13C/2H isotope labeling and MD simulation to a protein in three different crystal packing environments to shed light onto possible impact of packing on ring flips. The flips of the two Phe residues in ubiquitin, both surface exposed, appear remarkably conserved in the different crystal forms, even though the intermolecular packing is quite different: Phe4 flips on a ca. 10–20 ns time scale, and Phe45 are broadened in all crystals, presumably due to µs motion. Our findings suggest that intramolecular influences are more important for ring flips than intermolecular (packing) effects."}],"department":[{"_id":"PaSc"}],"article_processing_charge":"No","doi":"10.1016/j.yjsbx.2022.100079","oa":1,"intvolume":"         7","has_accepted_license":"1","ddc":["570"],"external_id":{"pmid":["36578472"]},"language":[{"iso":"eng"}],"_id":"12114","date_updated":"2026-07-20T09:49:12Z","file_date_updated":"2023-08-16T09:36:28Z","file":[{"relation":"main_file","file_name":"2023_JourStrucBiologyX_Gauto.pdf","success":1,"creator":"dernst","file_id":"14064","content_type":"application/pdf","date_created":"2023-08-16T09:36:28Z","checksum":"b4b1c10a31018aafe053b7d55a470e54","file_size":5132322,"access_level":"open_access","date_updated":"2023-08-16T09:36:28Z"}],"keyword":["Structural Biology"],"pmid":1,"fulldoi":"https://doi.org/10.1016/j.yjsbx.2022.100079","volume":7,"year":"2023","publisher":"Elsevier","month":"01","quality_controlled":"1","date_published":"2023-01-01T00:00:00Z","oa_version":"Published Version","title":"Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD","article_number":"100079","status":"public","publication_status":"published","publication":"Journal of Structural Biology: X","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["2590-1524"]},"related_material":{"record":[{"status":"public","relation":"dissertation_contains","id":"22334"}]},"acknowledgement":"The NMR platform in Grenoble is part of the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). This work was supported by the European Research Council (StG-2012-311318-ProtDyn2Function to P.S.) and used the platforms of the Grenoble Instruct Center (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) with support from FRISBI (ANR-10-INSB-05–02) and GRAL (ANR-10-LABX-49–01) within the Grenoble Partnership for Structural Biology (PSB). We would like to thank Sergei Izmailov for developing and maintaining the pyxmolpp2 library. N.R.S. acknowledges support from St. Petersburg State University in a form of the grant 92425251 and the access to the MRR, MCT and CAMR resource centers. P.S. thanks Malcolm Levitt for pointing out the fact that “tensor asymmetry” is better called “tensor biaxiality”.","citation":{"mla":"Gauto, Diego F., et al. “Aromatic Ring Flips in Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.” <i>Journal of Structural Biology: X</i>, vol. 7, 100079, Elsevier, 2023, doi:<a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">10.1016/j.yjsbx.2022.100079</a>.","chicago":"Gauto, Diego F., Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman Lichtenecker, Nikolai R. Skrynnikov, and Paul Schanda. “Aromatic Ring Flips in Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.” <i>Journal of Structural Biology: X</i>. Elsevier, 2023. <a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">https://doi.org/10.1016/j.yjsbx.2022.100079</a>.","ama":"Gauto DF, Lebedenko OO, Becker LM, et al. Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. <i>Journal of Structural Biology: X</i>. 2023;7. doi:<a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">10.1016/j.yjsbx.2022.100079</a>","ista":"Gauto DF, Lebedenko OO, Becker LM, Ayala I, Lichtenecker R, Skrynnikov NR, Schanda P. 2023. Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. 7, 100079.","ieee":"D. F. Gauto <i>et al.</i>, “Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD,” <i>Journal of Structural Biology: X</i>, vol. 7. Elsevier, 2023.","apa":"Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R., Skrynnikov, N. R., &#38; Schanda, P. (2023). Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. <i>Journal of Structural Biology: X</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">https://doi.org/10.1016/j.yjsbx.2022.100079</a>","short":"D.F. Gauto, O.O. Lebedenko, L.M. Becker, I. Ayala, R. Lichtenecker, N.R. Skrynnikov, P. Schanda, Journal of Structural Biology: X 7 (2023)."},"article_type":"original","day":"01","scopus_import":"1","date_created":"2023-01-12T11:55:38Z","corr_author":"1","tmp":{"short":"CC BY-NC-ND (4.0)","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)"},"type":"journal_article"},{"file_date_updated":"2024-01-30T12:36:39Z","file":[{"date_created":"2024-01-30T12:36:39Z","success":1,"file_name":"2023_CurrentOpinionStrucBio_Napoli.pdf","relation":"main_file","content_type":"application/pdf","file_id":"14907","creator":"dernst","access_level":"open_access","date_updated":"2024-01-30T12:36:39Z","checksum":"c850f7ac8a4234319755b672c1df69ae","file_size":1231998}],"date_updated":"2025-04-14T09:10:17Z","pmid":1,"fulldoi":"https://doi.org/10.1016/j.sbi.2023.102660","volume":82,"year":"2023","month":"10","publisher":"Elsevier","department":[{"_id":"PaSc"}],"abstract":[{"lang":"eng","text":"Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing itself as a powerful method for the characterization of protein dynamics at the atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling, and pulse sequence design has paved the way for quantitative analyses of even rare structural fluctuations. In addition to isotropic chemical-shift fluctuations exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has a wider arsenal of observables, allowing to see motions even if the exchanging states do not differ in their chemical shifts. We demonstrate the potential of the technique for probing motions in challenging large enzymes, membrane proteins, and protein assemblies."}],"article_processing_charge":"Yes (via OA deal)","doi":"10.1016/j.sbi.2023.102660","author":[{"orcid":"0000-0002-9043-136X","first_name":"Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","last_name":"Napoli","full_name":"Napoli, Federico"},{"orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","last_name":"Becker","full_name":"Becker, Lea Marie"},{"first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","last_name":"Schanda","full_name":"Schanda, Paul"}],"_id":"14036","issue":"10","oa":1,"intvolume":"        82","ddc":["570"],"external_id":{"pmid":["37536064"],"isi":["001053616200001"]},"language":[{"iso":"eng"}],"citation":{"short":"F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).","apa":"Napoli, F., Becker, L. M., &#38; Schanda, P. (2023). Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">https://doi.org/10.1016/j.sbi.2023.102660</a>","ieee":"F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle spinning relaxation dispersion NMR,” <i>Current Opinion in Structural Biology</i>, vol. 82, no. 10. Elsevier, 2023.","ista":"Napoli F, Becker LM, Schanda P. 2023. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 82(10), 102660.","ama":"Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. 2023;82(10). doi:<a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">10.1016/j.sbi.2023.102660</a>","chicago":"Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2023. <a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">https://doi.org/10.1016/j.sbi.2023.102660</a>.","mla":"Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>, vol. 82, no. 10, 102660, Elsevier, 2023, doi:<a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">10.1016/j.sbi.2023.102660</a>."},"project":[{"grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery"}],"acknowledgement":"We thank Petra Rovó for critical reading of this manuscript. We acknowledge the Austrian Science Foundation FWF (project AlloSpace, number I5812–B) and funding by the Institute of Science and Technology Austria.","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"type":"journal_article","article_type":"original","scopus_import":"1","date_created":"2023-08-13T22:01:11Z","day":"01","corr_author":"1","isi":1,"date_published":"2023-10-01T00:00:00Z","oa_version":"Published Version","title":"Protein dynamics detected by magic-angle spinning relaxation dispersion NMR","article_number":"102660","quality_controlled":"1","publication_identifier":{"issn":["0959-440X"],"eissn":["1879-033X"]},"status":"public","publication_status":"published","publication":"Current Opinion in Structural Biology","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"}]