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Direct observation of hierarchical protein dynamics

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Lewandowski, Józef R., Halse, M. E., Blackledge, Martin and Emsley, Lyndon (2015) Direct observation of hierarchical protein dynamics. Science, 348 (6234). pp. 578-581. doi:10.1126/science.aaa6111

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Official URL: http://dx.doi.org/10.1126/science.aaa6111

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Abstract

One of the fundamental challenges of physical biology is to understand the relationship between protein dynamics and function. At physiological temperatures, functional motions arise from the complex interplay of thermal motions of proteins and their environments. Here, we determine the hierarchy in the protein conformational energy landscape that underlies these motions, based on a series of temperature-dependent magic-angle spinning multinuclear nuclear-magnetic-resonance relaxation measurements in a hydrated nanocrystalline protein. The results support strong coupling between protein and solvent dynamics above 160 kelvin, with fast solvent motions, slow protein side-chain motions, and fast protein backbone motions being activated consecutively. Low activation energy, small-amplitude local motions dominate at low temperatures, with larger-amplitude, anisotropic, and functionally relevant motions involving entire peptide units becoming dominant at temperatures above 220 kelvin.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH): Proteins--Spectroscopic imaging
Journal or Publication Title: Science
Publisher: American Association for the Advancement of Science
ISSN: 0036-8075
Official Date: May 2015
Dates:
DateEvent
May 2015Published
24 March 2015Accepted
5 January 2015Submitted
Volume: 348
Number: 6234
Page Range: pp. 578-581
DOI: 10.1126/science.aaa6111
Status: Peer Reviewed
Publication Status: Published
Funder: France. Agence nationale de la recherche (ANR), Seventh Framework Programme (European Commission) (FP7), Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung [Swiss National Science Foundation] (SNSF), European Union International Reintegration Grant (IRG), University of Warwick
Grant number: PCV 2007 (ANR), BioNMR 261863 (FP7), 31-132857 (SNSF), PIRG03-GA-2008-231026 (IRG)

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