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Analytical Description of NMR Relaxation Highlights Correlated Dynamics in Intrinsically Disordered Proteins
Author(s) -
Salvi Nicola,
Abyzov Anton,
Blackledge Martin
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201706740
Subject(s) - intrinsically disordered proteins , libration (molecule) , dihedral angle , relaxation (psychology) , dynamics (music) , molecular dynamics , protein dynamics , chemical physics , function (biology) , nuclear magnetic resonance , physics , chemistry , statistical physics , computational chemistry , molecule , mathematics , biology , hydrogen bond , geometry , point (geometry) , evolutionary biology , acoustics , quantum mechanics , neuroscience
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.