{"oa":1,"oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2023-08-13T22:01:11Z","publisher":"Elsevier","scopus_import":"1","quality_controlled":"1","title":"Protein dynamics detected by magic-angle spinning relaxation dispersion NMR","status":"public","file":[{"date_updated":"2024-01-30T12:36:39Z","date_created":"2024-01-30T12:36:39Z","file_size":1231998,"file_id":"14907","success":1,"relation":"main_file","checksum":"c850f7ac8a4234319755b672c1df69ae","file_name":"2023_CurrentOpinionStrucBio_Napoli.pdf","access_level":"open_access","creator":"dernst","content_type":"application/pdf"}],"type":"journal_article","day":"01","article_processing_charge":"Yes (via OA deal)","month":"10","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"pmid":1,"date_updated":"2024-01-30T12:37:36Z","date_published":"2023-10-01T00:00:00Z","publication_status":"published","issue":"10","department":[{"_id":"PaSc"}],"abstract":[{"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.","lang":"eng"}],"intvolume":"        82","volume":82,"year":"2023","file_date_updated":"2024-01-30T12:36:39Z","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.","isi":1,"ddc":["570"],"project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery","grant_number":"I05812"}],"doi":"10.1016/j.sbi.2023.102660","author":[{"id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","full_name":"Napoli, Federico","first_name":"Federico","last_name":"Napoli","orcid":"0000-0002-9043-136X"},{"orcid":"0000-0002-6401-5151","last_name":"Becker","first_name":"Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie"},{"last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606"}],"publication":"Current Opinion in Structural Biology","external_id":{"isi":["001053616200001"],"pmid":["37536064"]},"publication_identifier":{"issn":["0959-440X"],"eissn":["1879-033X"]},"article_type":"original","citation":{"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.","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>.","short":"F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).","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>","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>","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>.","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."},"language":[{"iso":"eng"}],"article_number":"102660","_id":"14036"}