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• W2748943920 endingPage "14024" @default.
• W2748943920 startingPage "14020" @default.
• W2748943920 abstract "Abstract 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." @default.
• W2748943920 created "2017-08-31" @default.
• W2748943920 creator A5001250430 @default.
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• W2748943920 date "2017-09-14" @default.
• W2748943920 modified "2023-10-18" @default.
• W2748943920 title "Analytical Description of NMR Relaxation Highlights Correlated Dynamics in Intrinsically Disordered Proteins" @default.
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• W2748943920 doi "https://doi.org/10.1002/anie.201706740" @default.
• W2748943920 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28834051" @default.
• W2748943920 hasPublicationYear "2017" @default.
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