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|Title:||Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy||Authors:||Brath, U.
|Issue Date:||3-May-2006||Citation:||Brath, 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||Abstract:||Transverse 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.||Source Title:||Journal of the American Chemical Society||URI:||http://scholarbank.nus.edu.sg/handle/10635/100722||ISSN:||00027863||DOI:||10.1021/ja0570279|
|Appears in Collections:||Staff Publications|
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