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Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins


IBS researchers combine NMR and Molecular Dynamics to study the dynamics of intrinsically disordered proteins and develop a method for separating distinct contributions, describing different phenomena: fast vibrations of chemical bonds, local conformational transitions of the main chain , and rotation of the peptide planes.​

Published on 1 February 2018
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, the researchers of the FDP group (Protein Dynaics and Flexibility by NMR) 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 them to investigate the presence and extent of the correlated motions that are essential for function.


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