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Angew Chem Int Ed Engl. 2017 Nov 6;56(45):14020-14024. doi: 10.1002/anie.201706740. Epub 2017 Sep 14.

Analytical Description of NMR Relaxation Highlights Correlated Dynamics in Intrinsically Disordered Proteins.

Author information

1
Institut de Biologie Structurale, CNRS, CEA, UGA, Grenoble, France.

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.

KEYWORDS:

NMR spectroscopy; intrinsically disordered proteins; molecular dynamics simulation; protein dynamics; segmental motions

PMID:
28834051
DOI:
10.1002/anie.201706740
[Indexed for MEDLINE]

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