期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 56, 期 45, 页码 14020-14024出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201706740
关键词
intrinsically disordered proteins; molecular dynamics simulation; NMR spectroscopy; protein dynamics; segmental motions
资金
- Swiss National Science Foundation Early Postdoc.Mobility Fellowship [P2ELP2_148858]
- GENCI-TGCC [2016-077486, 2017-drfr1700]
- Swiss National Science Foundation (SNF) [P2ELP2_148858] Funding Source: Swiss National Science Foundation (SNF)
The dynamic fluctuations of intrinsically disordered proteins (IDPs) define their function. Although experimental nuclear magnetic resonance (NMR) relaxation reveals the motional complexity of these highly flexible proteins, the absence of physical models describing IDP dynamics hinders their mechanistic interpretation. Combining molecular dynamics simulation and NMR, we introduce a framework in which distinct motions are attributed to local libration, backbone dihedral angle dynamics and longer-range tumbling of one or more peptide planes. This model provides unique insight into segmental organization of dynamics in IDPs and allows us to investigate the presence and extent of the correlated motions that are essential for function.
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