{"month":"08","date_created":"2020-09-18T10:10:20Z","citation":{"ista":"Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. 2012. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. 134(36), 14800–14807.","chicago":"Tollinger, Martin, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst, and Paul Schanda. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2012. <a href=\"https://doi.org/10.1021/ja303591y\">https://doi.org/10.1021/ja303591y</a>.","apa":"Tollinger, M., Sivertsen, A. C., Meier, B. H., Ernst, M., &#38; Schanda, P. (2012). Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja303591y\">https://doi.org/10.1021/ja303591y</a>","mla":"Tollinger, Martin, et al. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.” <i>Journal of the American Chemical Society</i>, vol. 134, no. 36, American Chemical Society, 2012, pp. 14800–07, doi:<a href=\"https://doi.org/10.1021/ja303591y\">10.1021/ja303591y</a>.","ama":"Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. <i>Journal of the American Chemical Society</i>. 2012;134(36):14800-14807. doi:<a href=\"https://doi.org/10.1021/ja303591y\">10.1021/ja303591y</a>","short":"M. Tollinger, A.C. Sivertsen, B.H. Meier, M. Ernst, P. Schanda, Journal of the American Chemical Society 134 (2012) 14800–14807.","ieee":"M. Tollinger, A. C. Sivertsen, B. H. Meier, M. Ernst, and P. Schanda, “Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy,” <i>Journal of the American Chemical Society</i>, vol. 134, no. 36. American Chemical Society, pp. 14800–14807, 2012."},"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2012-08-21T00:00:00Z","day":"21","status":"public","article_type":"original","year":"2012","publisher":"American Chemical Society","page":"14800-14807","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0002-7863","1520-5126"]},"intvolume":"       134","extern":"1","type":"journal_article","date_updated":"2021-01-12T08:19:27Z","volume":134,"oa_version":"None","abstract":[{"lang":"eng","text":"We demonstrate that conformational exchange processes in proteins on microsecond-to-millisecond time scales can be detected and quantified by solid-state NMR spectroscopy. We show two independent approaches that measure the effect of conformational exchange on transverse relaxation parameters, namely Carr–Purcell–Meiboom–Gill relaxation-dispersion experiments and measurement of differential multiple-quantum coherence decay. Long coherence lifetimes, as required for these experiments, are achieved by the use of highly deuterated samples and fast magic-angle spinning. The usefulness of the approaches is demonstrated by application to microcrystalline ubiquitin. We detect a conformational exchange process in a region of the protein for which dynamics have also been observed in solution. Interestingly, quantitative analysis of the data reveals that the exchange process is more than 1 order of magnitude slower than in solution, and this points to the impact of the crystalline environment on free energy barriers."}],"issue":"36","publication":"Journal of the American Chemical Society","publication_status":"published","quality_controlled":"1","title":"Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy","_id":"8465","doi":"10.1021/ja303591y","author":[{"last_name":"Tollinger","full_name":"Tollinger, Martin","first_name":"Martin"},{"first_name":"Astrid C.","full_name":"Sivertsen, Astrid C.","last_name":"Sivertsen"},{"full_name":"Meier, Beat H.","first_name":"Beat H.","last_name":"Meier"},{"first_name":"Matthias","full_name":"Ernst, Matthias","last_name":"Ernst"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}]}