{"author":[{"last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul"},{"last_name":"Haran","full_name":"Haran, Gilad","first_name":"Gilad"}],"title":"NMR and single-molecule FRET insights into fast protein motions and their relation to function","license":"https://creativecommons.org/licenses/by/4.0/","has_accepted_license":"1","ddc":["570"],"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"01","type":"journal_article","pmid":1,"file":[{"relation":"main_file","success":1,"content_type":"application/pdf","access_level":"open_access","checksum":"c90861542ae3f9147939030d5bafed3c","date_updated":"2025-01-27T13:44:59Z","file_size":3025589,"file_name":"2024_AnnualReviews_Schanda.pdf","file_id":"18911","date_created":"2025-01-27T13:44:59Z","creator":"dernst"}],"abstract":[{"text":"Proteins often undergo large-scale conformational transitions, in which secondary and tertiary structure elements (loops, helices, and domains) change their structures or their positions with respect to each other. Simple considerations suggest that such dynamics should be relatively fast, but the functional cycles of many proteins are often relatively slow. Sophisticated experimental methods are starting to tackle this dichotomy and shed light on the contribution of large-scale conformational dynamics to protein function. In this review, we focus on the contribution of single-molecule Förster resonance energy transfer and nuclear magnetic resonance (NMR) spectroscopies to the study of conformational dynamics. We briefly describe the state of the art in each of these techniques and then point out their similarities and differences, as well as the relative strengths and weaknesses of each. Several case studies, in which the connection between fast conformational dynamics and slower function has been demonstrated, are then introduced and discussed. These examples include both enzymes and large protein machines, some of which have been studied by both NMR and fluorescence spectroscopies.","lang":"eng"}],"file_date_updated":"2025-01-27T13:44:59Z","department":[{"_id":"PaSc"}],"article_type":"original","citation":{"ama":"Schanda P, Haran G. NMR and single-molecule FRET insights into fast protein motions and their relation to function. <i>Annual Review of Biophysics</i>. 2024;53:247-273. doi:<a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">10.1146/annurev-biophys-070323-022428</a>","short":"P. Schanda, G. Haran, Annual Review of Biophysics 53 (2024) 247–273.","ieee":"P. Schanda and G. Haran, “NMR and single-molecule FRET insights into fast protein motions and their relation to function,” <i>Annual Review of Biophysics</i>, vol. 53. Annual Reviews, pp. 247–273, 2024.","chicago":"Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function.” <i>Annual Review of Biophysics</i>. Annual Reviews, 2024. <a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">https://doi.org/10.1146/annurev-biophys-070323-022428</a>.","apa":"Schanda, P., &#38; Haran, G. (2024). NMR and single-molecule FRET insights into fast protein motions and their relation to function. <i>Annual Review of Biophysics</i>. Annual Reviews. <a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">https://doi.org/10.1146/annurev-biophys-070323-022428</a>","mla":"Schanda, Paul, and Gilad Haran. “NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function.” <i>Annual Review of Biophysics</i>, vol. 53, Annual Reviews, 2024, pp. 247–73, doi:<a href=\"https://doi.org/10.1146/annurev-biophys-070323-022428\">10.1146/annurev-biophys-070323-022428</a>.","ista":"Schanda P, Haran G. 2024. NMR and single-molecule FRET insights into fast protein motions and their relation to function. Annual Review of Biophysics. 53, 247–273."},"publication_identifier":{"issn":["1936-122X"],"eissn":["1936-1238"]},"_id":"18910","language":[{"iso":"eng"}],"publication_status":"published","quality_controlled":"1","scopus_import":"1","year":"2024","oa_version":"Published Version","project":[{"grant_number":"I05812","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","name":"AlloSpace. The emergence and mechanisms of allostery"}],"date_created":"2025-01-27T13:40:34Z","date_updated":"2025-01-27T13:46:22Z","oa":1,"date_published":"2024-07-01T00:00:00Z","OA_type":"hybrid","acknowledgement":"G.H. is the incumbent of the Hilda Pomeraniec Memorial Professorial Chair. He has been partially funded by the European Research Council under the European Union's Horizon 2020 research and innovation program (grant 742637, SMALLOSTERY), by National Science Foundation–US-Israel Binational Science Foundation grant 2021700, and by an Israel Science Foundation Breakthrough grant (1924/22). P.S. acknowledges funding from the Austrian Science Fund (project “AlloSpace,” I05812) and intramural funding from the Institute of Science and Technology Austria.","publisher":"Annual Reviews","month":"07","doi":"10.1146/annurev-biophys-070323-022428","OA_place":"publisher","status":"public","page":"247-273","publication":"Annual Review of Biophysics","volume":53,"corr_author":"1","intvolume":"        53","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"external_id":{"pmid":["38346243"]}}