Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja0570279
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dc.titleFunctional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy
dc.contributor.authorBrath, U.
dc.contributor.authorAkke, M.
dc.contributor.authorYang, D.
dc.contributor.authorKay, L.E.
dc.contributor.authorMulder, F.A.A.
dc.date.accessioned2014-10-27T08:28:59Z
dc.date.available2014-10-27T08:28:59Z
dc.date.issued2006-05-03
dc.identifier.citationBrath, U., Akke, M., Yang, D., Kay, L.E., Mulder, F.A.A. (2006-05-03). Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society 128 (17) : 5718-5727. ScholarBank@NUS Repository. https://doi.org/10.1021/ja0570279
dc.identifier.issn00027863
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100722
dc.description.abstractTransverse relaxation dispersion NMR spectroscopy can provide atom-specific information about time scales, populations, and the extent of structural reorganization in proteins under equilibrium conditions. A method is described that uses side-chain methyl groups as local reporters for conformational transitions taking place in the microsecond regime. The experiment measures carbon nuclear spin relaxation rates in the presence of continuous wave off-resonance irradiation, in proteins uniformly enriched with 13C, and partially randomly labeled with 2H. The method was applied to human FK-506 binding protein (FKBP12), which uses a common surface for binding substrates in its dual role as both an immunophilin and folding assistant. Conformational dynamics on a time scale of ∼130 μs were detected for methyl groups located in the substrate binding pocket, demonstrating its plasticity in the absence of substrate. The spatial arrangement of affected side-chain atoms suggests that substrate recognition involves the rapid relative movement of the subdomain comprising residues Ala81-Thr96 and that the observed dynamics play an important role in facilitating the interaction of this protein with its many partners, including calcineurin. © 2006 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ja0570279
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/ja0570279
dc.description.sourcetitleJournal of the American Chemical Society
dc.description.volume128
dc.description.issue17
dc.description.page5718-5727
dc.description.codenJACSA
dc.identifier.isiut000237389900042
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