{"file_date_updated":"2025-11-17T11:54:17Z","project":[{"grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0"}],"user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","corr_author":"1","date_updated":"2025-11-18T09:55:19Z","tmp":{"short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"title":"Data for \"Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes\"","abstract":[{"lang":"eng","text":"Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. "}],"author":[{"full_name":"Becker, Lea Marie","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","last_name":"Becker","first_name":"Lea Marie"},{"orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul"}],"publisher":"Institute of Science and Technology Austria","oa_version":"None","oa":1,"acknowledgement":"We thank Nikolai R. Skrynnikov and Olga O. Lebedenko (St. Petersburg) for insightful discussions and for performing exploratory MD simulations. We are grateful to Tobias Schubeis (Lyon) for advice with GB1 crystallization, and Rebecca Schmid for initial crystallization trials.\r\nWe thank Sebastian Falkner for assistance with constructing the structural model of the IgG:GB1 complex.\r\nThis research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance and the Lab Support Facilities. We thank Petra Rovó and Margarita Valhondo Falcón for excellent support of the NMR facility.\r\nLea M. Becker is recipient of a DOC fellowship of the Austrian Academy of Sciences at the Institute of Science and Technology Austria (grant no. PR10660EAW01). Christophe Chipot acknowledges the European Research Council (grant project 101097272 ``MilliInMicro'') and the Métropole du Grand Nancy (grant project ``ARC''). BM07-FIP2 is supported by the French ANR PIA3 (France 2030) EquipEx+ project MAGNIFIX under grant agreement ANR-21-ESRE-0011.","day":"18","status":"public","ddc":["572"],"citation":{"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>.","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>","short":"L.M. Becker, P. Schanda, (2025).","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.","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>.","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>"},"year":"2025","date_created":"2025-11-13T09:29:58Z","has_accepted_license":"1","date_published":"2025-11-18T00:00:00Z","type":"research_data","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"month":"11","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"contributor":[{"contributor_type":"researcher","first_name":"Haohao ","last_name":"Fu"},{"id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman","contributor_type":"researcher","first_name":"Benjamin"},{"last_name":"Dreydoppel","first_name":"Matthias","contributor_type":"researcher"},{"first_name":"Anna","contributor_type":"researcher","last_name":"Kapitonova","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471"},{"first_name":"Daniel","contributor_type":"researcher","last_name":"Balazs","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","orcid":"0000-0001-7597-043X"},{"last_name":"Weininger","contributor_type":"researcher","first_name":"Ulrich"},{"last_name":"Engilberge","contributor_type":"researcher","first_name":"Sylvain"},{"contributor_type":"researcher","first_name":"Christophe","last_name":"Chipot"}],"_id":"20641","article_processing_charge":"No","file":[{"file_name":"Research_Data.zip","content_type":"application/zip","file_size":1806589513,"date_updated":"2025-11-13T09:38:35Z","relation":"main_file","date_created":"2025-11-13T09:38:35Z","file_id":"20643","checksum":"a73a0550c644957e7f62241e239d3a1d","creator":"lbecker","access_level":"open_access"},{"file_size":191376,"date_updated":"2025-11-17T11:54:17Z","date_created":"2025-11-17T11:54:17Z","relation":"table_of_contents","file_name":"README.pdf","content_type":"application/pdf","creator":"lbecker","access_level":"open_access","file_id":"20652","checksum":"7176b257f753c213a0460ee06f802363"}],"doi":"10.15479/AT-ISTA-20641"}