[{"oa":1,"article_processing_charge":"Yes (via OA deal)","title":"Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches","scopus_import":"1","publication":"Progress in Nuclear Magnetic Resonance Spectroscopy","year":"2026","status":"public","_id":"22974","month":"09","publication_identifier":{"issn":["0079-6565"],"eissn":["1873-3301"]},"license":"https://creativecommons.org/licenses/by/4.0/","day":"01","fulldoi":"https://doi.org/10.1016/j.pnmrs.2026.101615","ddc":["540"],"publisher":"Elsevier","doi":"10.1016/j.pnmrs.2026.101615","OA_place":"publisher","author":[{"full_name":"Tatman, Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","first_name":"Benjamin","last_name":"Tatman"},{"last_name":"Schanda","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul"}],"abstract":[{"text":"Far from being static structures, it is now well accepted that proteins are highly dynamic entities even in the solid state. Here, we review recent progress in application of magic-angle spinning (MAS) NMR for studying the site-specific dynamics of proteins, as assessed using spin-relaxation and measurement of anisotropic spin interactions. We focus on the types of experimental data that are available, and how best to access the information which is provided by these experimental measurements; in particular, we provide a retrospective on the field in light of recent advances in analytical methodologies, which have led to a slow paradigm shift in how we interpret relaxation rate constant measurements made in the solid state.","lang":"eng"}],"OA_type":"hybrid","keyword":["Solid-state NMR","Protein dynamics","Magic-angle spinning"],"article_number":"101615","corr_author":"1","das_tickbox":"1","oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2026-09-22T05:44:22Z","language":[{"iso":"eng"}],"quality_controlled":"1","has_accepted_license":"1","dataavailabilitystatement":"No data was used for the research described in the article.","type":"journal_article","researchdata_availability":"no","date_published":"2026-09-01T00:00:00Z","date_updated":"2026-10-06T13:00:47Z","supplementarymaterial":"yes","department":[{"_id":"PaSc"}],"publication_status":"epub_ahead","tmp":{"image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"article_type":"original","volume":"156-157","acknowledgement":"We thank the Austrian Science Fund (FWF, project number 10.55776/I5812) for support. We are grateful to Petra Rovó (ISTA) for many insightful discussions.","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}],"citation":{"chicago":"Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics by Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier, 2026. <a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">https://doi.org/10.1016/j.pnmrs.2026.101615</a>.","short":"B. Tatman, P. Schanda, Progress in Nuclear Magnetic Resonance Spectroscopy 156–157 (2026).","ieee":"B. Tatman and P. Schanda, “Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches,” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157. Elsevier, 2026.","mla":"Tatman, Benjamin, and Paul Schanda. “Quantifying Fast Protein Dynamics by Magic-Angle Spinning NMR: Progress in Experimental and Analytical Approaches.” <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>, vol. 156–157, 101615, Elsevier, 2026, doi:<a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">10.1016/j.pnmrs.2026.101615</a>.","apa":"Tatman, B., &#38; Schanda, P. (2026). Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">https://doi.org/10.1016/j.pnmrs.2026.101615</a>","ista":"Tatman B, Schanda P. 2026. Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. Progress in Nuclear Magnetic Resonance Spectroscopy. 156–157, 101615.","ama":"Tatman B, Schanda P. Quantifying fast protein dynamics by magic-angle spinning NMR: Progress in experimental and analytical approaches. <i>Progress in Nuclear Magnetic Resonance Spectroscopy</i>. 2026;156-157. doi:<a href=\"https://doi.org/10.1016/j.pnmrs.2026.101615\">10.1016/j.pnmrs.2026.101615</a>"},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.pnmrs.2026.101615"}]}]