[{"citation":{"ieee":"V. Sunko and J. Orenstein, “Linear magneto-birefringence as a probe of altermagnetism,” <i>npj Quantum Materials</i>. Springer Nature, 2026.","ista":"Sunko V, Orenstein J. 2026. Linear magneto-birefringence as a probe of altermagnetism. npj Quantum Materials.","mla":"Sunko, Veronika, and J. Orenstein. “Linear Magneto-Birefringence as a Probe of Altermagnetism.” <i>Npj Quantum Materials</i>, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41535-026-00901-8\">10.1038/s41535-026-00901-8</a>.","ama":"Sunko V, Orenstein J. Linear magneto-birefringence as a probe of altermagnetism. <i>npj Quantum Materials</i>. 2026. doi:<a href=\"https://doi.org/10.1038/s41535-026-00901-8\">10.1038/s41535-026-00901-8</a>","chicago":"Sunko, Veronika, and J. Orenstein. “Linear Magneto-Birefringence as a Probe of Altermagnetism.” <i>Npj Quantum Materials</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41535-026-00901-8\">https://doi.org/10.1038/s41535-026-00901-8</a>.","apa":"Sunko, V., &#38; Orenstein, J. (2026). Linear magneto-birefringence as a probe of altermagnetism. <i>Npj Quantum Materials</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41535-026-00901-8\">https://doi.org/10.1038/s41535-026-00901-8</a>","short":"V. Sunko, J. Orenstein, Npj Quantum Materials (2026)."},"publication_status":"epub_ahead","author":[{"last_name":"Sunko","full_name":"Sunko, Veronika","id":"23cb1cf6-2c7a-11ef-91a4-f72fc19f20b3","first_name":"Veronika","orcid":"0000-0003-2724-3523"},{"first_name":"J.","last_name":"Orenstein","full_name":"Orenstein, J."}],"day":"30","publisher":"Springer Nature","OA_place":"publisher","doi":"10.1038/s41535-026-00901-8","month":"05","article_type":"original","oa_version":"Published Version","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41535-026-00901-8"}],"ddc":["530"],"arxiv":1,"publication_identifier":{"eissn":["2397-4648"]},"acknowledgement":"We thank Nicola Spaldin and Marc Vila for valuable discussions. J.O. received support from the Quantum Materials (KC2202) program under the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences, Materials Sciences and Engineering Division under Contract No. DE-AC02-05CH11231, and the Gordon and Betty Moore Foundation's EPiQS Initiative through Grant GBMF4537 to J.O. at UC Berkeley.","date_created":"2026-03-11T10:40:08Z","publication":"npj Quantum Materials","year":"2026","date_updated":"2026-06-24T10:31:05Z","abstract":[{"text":"Altermagnets are a class of collinear magnets that exhibit non-relativistic spin splitting (NRSS) of electronic bands in the absence of net magnetization. Their potential to generate large spin polarization without spin-orbit coupling has created strong interest in probes that access the underlying order parameter directly. In this Perspective, we show that linear magneto-birefringence (LMB) provides a natural and broadly applicable route to detecting altermagnetic order. Building on the correspondence between the momentum-space structure of NRSS and the ferroic ordering of magnetic multipoles in real space, we demonstrate how $d$-wave and $g$-wave NRSS textures yield distinct LMB responses. We present a symmetry-based framework that identifies the optical geometries and field configurations required to isolate specific multipole components, enabling domain imaging and providing benchmarks for theoretical models of LMB.","lang":"eng"}],"external_id":{"arxiv":["2511.16421"]},"department":[{"_id":"VeSu"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","corr_author":"1","oa":1,"OA_type":"gold","language":[{"iso":"eng"}],"title":"Linear magneto-birefringence as a probe of altermagnetism","article_processing_charge":"Yes","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)"},"date_published":"2026-05-30T00:00:00Z","_id":"21437","type":"journal_article","has_accepted_license":"1"},{"file":[{"creator":"dernst","checksum":"b660048bb271f24d6763803e247d5c32","success":1,"file_name":"2026_NatureComm_Svoboda.pdf","relation":"main_file","access_level":"open_access","file_size":1068919,"content_type":"application/pdf","date_updated":"2026-06-24T06:50:24Z","file_id":"22136","date_created":"2026-06-24T06:50:24Z"}],"citation":{"ieee":"J. Svoboda, H. Nemati, J. Tkadlec, K. Kaveh, and K. Chatterjee, “The effect of the fitness gradient on fixation probability,” <i>Nature Communications</i>, vol. 17. Springer Nature, 2026.","apa":"Svoboda, J., Nemati, H., Tkadlec, J., Kaveh, K., &#38; Chatterjee, K. (2026). The effect of the fitness gradient on fixation probability. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-026-71777-2\">https://doi.org/10.1038/s41467-026-71777-2</a>","short":"J. Svoboda, H. Nemati, J. Tkadlec, K. Kaveh, K. Chatterjee, Nature Communications 17 (2026).","mla":"Svoboda, Jakub, et al. “The Effect of the Fitness Gradient on Fixation Probability.” <i>Nature Communications</i>, vol. 17, 5325, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41467-026-71777-2\">10.1038/s41467-026-71777-2</a>.","ista":"Svoboda J, Nemati H, Tkadlec J, Kaveh K, Chatterjee K. 2026. The effect of the fitness gradient on fixation probability. Nature Communications. 17, 5325.","chicago":"Svoboda, Jakub, Hossein Nemati, Josef Tkadlec, Kamran Kaveh, and Krishnendu Chatterjee. “The Effect of the Fitness Gradient on Fixation Probability.” <i>Nature Communications</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41467-026-71777-2\">https://doi.org/10.1038/s41467-026-71777-2</a>.","ama":"Svoboda J, Nemati H, Tkadlec J, Kaveh K, Chatterjee K. The effect of the fitness gradient on fixation probability. <i>Nature Communications</i>. 2026;17. doi:<a href=\"https://doi.org/10.1038/s41467-026-71777-2\">10.1038/s41467-026-71777-2</a>"},"publication_status":"published","ec_funded":1,"scopus_import":"1","DOAJ_listed":"1","author":[{"id":"130759D2-D7DD-11E9-87D2-DE0DE6697425","first_name":"Jakub","orcid":"0000-0002-1419-3267","last_name":"Svoboda","full_name":"Svoboda, Jakub"},{"first_name":"Hossein","full_name":"Nemati, Hossein","last_name":"Nemati"},{"full_name":"Tkadlec, Josef","last_name":"Tkadlec","orcid":"0000-0002-1097-9684","first_name":"Josef","id":"3F24CCC8-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Kaveh","full_name":"Kaveh, Kamran","first_name":"Kamran"},{"last_name":"Chatterjee","full_name":"Chatterjee, Krishnendu","id":"2E5DCA20-F248-11E8-B48F-1D18A9856A87","first_name":"Krishnendu","orcid":"0000-0002-4561-241X"}],"day":"01","publisher":"Springer Nature","project":[{"call_identifier":"H2020","grant_number":"863818","_id":"0599E47C-7A3F-11EA-A408-12923DDC885E","name":"Formal Methods for Stochastic Models: Algorithms and Applications"}],"volume":17,"OA_place":"publisher","quality_controlled":"1","doi":"10.1038/s41467-026-71777-2","article_type":"original","month":"12","oa_version":"Published Version","status":"public","article_number":"5325","researchdata_availability":"no","ddc":["000"],"acknowledgement":"J.S. and K.C. were supported by the European Research Council (ERC)\r\nCoG 863818 (ForM-SMArt) and Austrian Science Fund (FWF) 10.55776/\r\nCOE12. J.T. was supported by GAČR grant 25-17377S and by Charles\r\nUniv. projects UNCE 24/SCI/008 and PRIMUS 24/SCI/012.","publication_identifier":{"eissn":["2041-1723"]},"date_updated":"2026-06-24T07:53:53Z","year":"2026","publication":"Nature Communications","date_created":"2026-06-21T22:02:59Z","abstract":[{"lang":"eng","text":"Evolutionary biology examines how the genetic and phenotypic composition\r\nof populations changes over time. An important goal is to determine the\r\nfixation probability of a single advantageous mutant that arises in a homogeneous\r\npopulation of N residents. Many real populations experience environmental\r\ngradients that cause mutations to be beneficial in some spatial\r\nregions but harmful in others. Here, we study the fixation probability of a\r\nmutant placed on a simple one-dimensional spatial structure that experiences\r\nsuch a gradient. The mutant’s fitness varies linearly from1 − s to 1 + s, whereas\r\nthe resident fitness is constant and equal to 1. The existing literature suggests\r\nthat such heterogeneity in the mutant’s fitness should lead to a decrease in its\r\nfixation probability. However, in this work, we find that small, non-negligible\r\ngradients (s < 1=√N) substantially increase the fixation probability,while larger\r\ngradients (s > (log N)/√N) substantially decrease it.Moreover, we quantify the\r\nstrength of this phenomenon analytically and we precisely delimit the range of\r\nthe gradients for which it occurs. Our computer simulations closely match\r\nthose findings. Altogether, our results indicate that subjecting a simple\r\npopulation structure to natural environmental conditions can produce strong\r\ncounterintuitive effects."}],"external_id":{"pmid":["41997932"]},"department":[{"_id":"KrCh"}],"oa":1,"supplementarymaterial":"yes","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","corr_author":"1","OA_type":"gold","dataavailabilitystatement":"Correspondence and requests for materials should be addressed to Krishnendu Chatterjee.","language":[{"iso":"eng"}],"file_date_updated":"2026-06-24T06:50:24Z","das_tickbox":"0","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)"},"title":"The effect of the fitness gradient on fixation probability","article_processing_charge":"Yes","date_published":"2026-12-01T00:00:00Z","pmid":1,"intvolume":"        17","type":"journal_article","_id":"22101","has_accepted_license":"1"},{"_id":"22103","type":"conference","intvolume":"         5","date_published":"2026-04-01T00:00:00Z","das_tickbox":"0","title":"Explaining decisions one conversation at a time: Opportunities and risks of LLMs as explainability assistants","article_processing_charge":"No","language":[{"iso":"eng"}],"OA_type":"green","oa":1,"supplementarymaterial":"no","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","corr_author":"1","department":[{"_id":"ToHe"}],"abstract":[{"lang":"eng","text":"Modern AI systems increasingly rely on opaque, highly complex models whose inner workings remain inaccessible even to experts. This opacity creates challenges for trust, accountability, and compliance with\r\nemerging regulatory expectations such as the “right to an explanation”. While traditional explainability methods—feature attributions, counterfactuals, surrogate models—and interpretable model classes provide valuable insights for engineers, they often fall short of delivering the contextual, conversational explanations that\r\nreal users expect. Large Language Models (LLMs) offer a promising new avenue for explanation due to their\r\nability to engage interactively, adapt to user needs, and translate technical outputs into more accessible reasoning. However, their tendencies toward hallucination, conflict avoidance, and oversimplification introduce\r\nserious risks when used as explanatory agents. This paper analyzes these opportunities and limitations, examines verification strategies for ensuring explanation fidelity, and situates LLM-generated explanations within\r\nbroader concerns about public trust. The paper concludes by outlining best practices and future research directions for building robust, verifiable, and human-aligned explanation systems."}],"year":"2026","date_updated":"2026-06-24T08:37:00Z","date_created":"2026-06-21T22:03:00Z","publication":"Proceedings of the 18th International Conference on Agents and Artificial Intelligence","acknowledgement":"This work has been supported by the European Research Council under Grant No.: ERC-2020-AdG\r\n101020093. LLM–based tools have been used as\r\nwriting assistance to help improve presentation.\r\n","publication_identifier":{"issn":["2184-3589"],"eissn":["2184-433X"],"isbn":["9789897587962"]},"keyword":["Explainable AI","Large Language Models","Trust in AI"],"researchdata_availability":"no","status":"public","main_file_link":[{"open_access":"1","url":"https://filipcano.org/files/icaart26llm.pdf"}],"oa_version":"Accepted Version","conference":{"location":"Marbella, Spain","end_date":"2026-03-08","name":"ICAART: International Conference on Agents and Artificial Intelligence","start_date":"2026-03-05"},"month":"04","quality_controlled":"1","doi":"10.5220/0014483200004052","OA_place":"repository","volume":5,"publisher":"Science and Technology Publications","project":[{"_id":"62781420-2b32-11ec-9570-8d9b63373d4d","grant_number":"101020093","call_identifier":"H2020","name":"Vigilant Algorithmic Monitoring of Software"}],"day":"01","author":[{"orcid":"0000-0002-0783-904X","first_name":"Filip","id":"708cad98-e86a-11ef-8098-bdae2d7c6af1","full_name":"Cano Cordoba, Filip","last_name":"Cano Cordoba"}],"scopus_import":"1","ec_funded":1,"page":"4689-4696","publication_status":"published","citation":{"ieee":"F. Cano Cordoba, “Explaining decisions one conversation at a time: Opportunities and risks of LLMs as explainability assistants,” in <i>Proceedings of the 18th International Conference on Agents and Artificial Intelligence</i>, Marbella, Spain, 2026, vol. 5, pp. 4689–4696.","apa":"Cano Cordoba, F. (2026). Explaining decisions one conversation at a time: Opportunities and risks of LLMs as explainability assistants. In <i>Proceedings of the 18th International Conference on Agents and Artificial Intelligence</i> (Vol. 5, pp. 4689–4696). Marbella, Spain: Science and Technology Publications. <a href=\"https://doi.org/10.5220/0014483200004052\">https://doi.org/10.5220/0014483200004052</a>","short":"F. Cano Cordoba, in:, Proceedings of the 18th International Conference on Agents and Artificial Intelligence, Science and Technology Publications, 2026, pp. 4689–4696.","ama":"Cano Cordoba F. Explaining decisions one conversation at a time: Opportunities and risks of LLMs as explainability assistants. In: <i>Proceedings of the 18th International Conference on Agents and Artificial Intelligence</i>. Vol 5. Science and Technology Publications; 2026:4689-4696. doi:<a href=\"https://doi.org/10.5220/0014483200004052\">10.5220/0014483200004052</a>","mla":"Cano Cordoba, Filip. “Explaining Decisions One Conversation at a Time: Opportunities and Risks of LLMs as Explainability Assistants.” <i>Proceedings of the 18th International Conference on Agents and Artificial Intelligence</i>, vol. 5, Science and Technology Publications, 2026, pp. 4689–96, doi:<a href=\"https://doi.org/10.5220/0014483200004052\">10.5220/0014483200004052</a>.","chicago":"Cano Cordoba, Filip. “Explaining Decisions One Conversation at a Time: Opportunities and Risks of LLMs as Explainability Assistants.” In <i>Proceedings of the 18th International Conference on Agents and Artificial Intelligence</i>, 5:4689–96. Science and Technology Publications, 2026. <a href=\"https://doi.org/10.5220/0014483200004052\">https://doi.org/10.5220/0014483200004052</a>.","ista":"Cano Cordoba F. 2026. Explaining decisions one conversation at a time: Opportunities and risks of LLMs as explainability assistants. Proceedings of the 18th International Conference on Agents and Artificial Intelligence. ICAART: International Conference on Agents and Artificial Intelligence vol. 5, 4689–4696."}},{"day":"10","related_material":{"record":[{"status":"public","relation":"research_data","id":"20641"},{"relation":"research_data","status":"public","id":"21145"}]},"author":[{"last_name":"Becker","full_name":"Becker, Lea Marie","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie"},{"full_name":"Fu, Haohao","last_name":"Fu","first_name":"Haohao"},{"full_name":"Tatman, Benjamin","last_name":"Tatman","first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f"},{"first_name":"Matthias","last_name":"Dreydoppel","full_name":"Dreydoppel, Matthias"},{"first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471","last_name":"Kapitonova","full_name":"Kapitonova, Anna"},{"first_name":"Daniel","id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","orcid":"0000-0001-7597-043X","full_name":"Balazs, Daniel","last_name":"Balazs"},{"first_name":"Ulrich","last_name":"Weininger","full_name":"Weininger, Ulrich"},{"full_name":"Engilberge, Sylvain","last_name":"Engilberge","first_name":"Sylvain"},{"first_name":"Christophe","full_name":"Chipot, Christophe","last_name":"Chipot"},{"first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","last_name":"Schanda"}],"publisher":"Springer Nature","project":[{"_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777","name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches"}],"publication_status":"epub_ahead","citation":{"ieee":"L. M. Becker <i>et al.</i>, “Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes,” <i>Nature Chemistry</i>. Springer Nature, 2026.","apa":"Becker, L. M., Fu, H., Tatman, B., Dreydoppel, M., Kapitonova, A., Balazs, D., … Schanda, P. (2026). Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>","short":"L.M. Becker, H. Fu, B. Tatman, M. Dreydoppel, A. Kapitonova, D. Balazs, U. Weininger, S. Engilberge, C. Chipot, P. Schanda, Nature Chemistry (2026).","chicago":"Becker, Lea Marie, Haohao Fu, Benjamin Tatman, Matthias Dreydoppel, Anna Kapitonova, Daniel Balazs, Ulrich Weininger, Sylvain Engilberge, Christophe Chipot, and Paul Schanda. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41557-026-02155-0\">https://doi.org/10.1038/s41557-026-02155-0</a>.","mla":"Becker, Lea Marie, et al. “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” <i>Nature Chemistry</i>, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>.","ama":"Becker LM, Fu H, Tatman B, et al. Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. <i>Nature Chemistry</i>. 2026. doi:<a href=\"https://doi.org/10.1038/s41557-026-02155-0\">10.1038/s41557-026-02155-0</a>","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."},"scopus_import":"1","oa_version":"Published Version","month":"06","article_type":"original","ddc":["540"],"researchdata_availability":"yes","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41557-026-02155-0"}],"OA_place":"publisher","doi":"10.1038/s41557-026-02155-0","quality_controlled":"1","department":[{"_id":"PaSc"},{"_id":"LifeSc"}],"corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","supplementarymaterial":"yes","oa":1,"date_created":"2026-06-21T22:03:01Z","publication":"Nature Chemistry","year":"2026","date_updated":"2026-06-24T08:47:58Z","publication_identifier":{"eissn":["17554349"],"issn":["17554330"]},"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).","PlanS_conform":"1","external_id":{"pmid":["42271006"]},"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."}],"has_accepted_license":"1","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"_id":"22105","type":"journal_article","language":[{"iso":"eng"}],"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.","OA_type":"hybrid","pmid":1,"date_published":"2026-06-10T00:00:00Z","article_processing_charge":"Yes (via OA deal)","title":"Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes","das_tickbox":"1","tmp":{"short":"CC BY (4.0)","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"}},{"project":[{"name":"Exploring protein dynamics by solid-state MAS NMR through specific labeling approaches","_id":"7be609c4-9f16-11ee-852c-85015ce2b9b0","grant_number":"26777"}],"publisher":"Institute of Science and Technology Austria","day":"09","related_material":{"record":[{"relation":"earlier_version","status":"public","id":"20641"},{"id":"22105","status":"public","relation":"used_in_publication"}]},"author":[{"id":"36336939-eb97-11eb-a6c2-c83f1214ca79","first_name":"Lea Marie","orcid":"0000-0002-6401-5151","last_name":"Becker","full_name":"Becker, Lea Marie"},{"full_name":"Schanda, Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606"},{"full_name":"Chipot, Christophe","last_name":"Chipot","first_name":"Christophe"}],"contributor":[{"contributor_type":"researcher","last_name":"Fu","first_name":"Haohao"},{"first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman","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"},{"id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","first_name":"Daniel","orcid":"0000-0001-7597-043X","contributor_type":"researcher","last_name":"Balazs"},{"first_name":"Ulrich","last_name":"Weininger","contributor_type":"researcher"},{"contributor_type":"researcher","last_name":"Engilberge","first_name":"Sylvain"}],"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.","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>","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>.","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>.","mla":"Becker, Lea Marie, et al. <i>Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.”</i> Institute of Science and Technology Austria, 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-21145\">10.15479/AT-ISTA-21145</a>.","apa":"Becker, L. M., Schanda, P., &#38; Chipot, C. (2026). Additional Data for “Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes.” Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-21145\">https://doi.org/10.15479/AT-ISTA-21145</a>","short":"L.M. Becker, P. Schanda, C. Chipot, (2026)."},"file":[{"checksum":"02a419cce8cea450bc952f35488d2df5","creator":"lbecker","content_type":"text/plain","date_created":"2026-02-05T13:52:37Z","file_id":"21146","date_updated":"2026-02-05T13:52:37Z","file_name":"README.txt","access_level":"open_access","relation":"table_of_contents","file_size":4263},{"creator":"lbecker","checksum":"b0b82b1aa73985b0b308a3fa52d21aea","success":1,"file_name":"Research_Data.zip","access_level":"open_access","file_size":50647107,"relation":"main_file","content_type":"application/zip","file_id":"21147","date_updated":"2026-02-05T13:52:41Z","date_created":"2026-02-05T13:52:41Z"}],"ddc":["572"],"status":"public","oa_version":"Published Version","month":"02","doi":"10.15479/AT-ISTA-21145","corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"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"}],"date_created":"2026-02-05T13:54:39Z","date_updated":"2026-06-24T08:47:57Z","year":"2026","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.","has_accepted_license":"1","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"_id":"21145","type":"research_data","date_published":"2026-02-09T00:00:00Z","article_processing_charge":"No","title":"Additional Data for \"Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes\"","tmp":{"image":"/images/cc_by_nc.png","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","short":"CC BY-NC (4.0)","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"file_date_updated":"2026-02-05T13:52:41Z"}]