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Protein dynamics. Direct observation of hierarchical protein dynamics.

  • Lewandowski JR Université de Lyon, Institut de Sciences Analytiques (CNRS/ENS-Lyon/UCB-Lyon 1), Centre de Résonance Magnétique Nucléaire à Très Hauts Champs, 69100 Villeurbanne, France. j.r.lewandowski@warwick.ac.uk martin.blackledge@ibs.fr lyndon.emsley@epfl.ch.
  • Halse ME Université de Lyon, Institut de Sciences Analytiques (CNRS/ENS-Lyon/UCB-Lyon 1), Centre de Résonance Magnétique Nucléaire à Très Hauts Champs, 69100 Villeurbanne, France.
  • Blackledge M Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38044 Grenoble, France; CNRS, IBS, F-38044 Grenoble, France; CEA, IBS, F-38044 Grenoble, France. j.r.lewandowski@warwick.ac.uk martin.blackledge@ibs.fr lyndon.emsley@epfl.ch.
  • Emsley L Université de Lyon, Institut de Sciences Analytiques (CNRS/ENS-Lyon/UCB-Lyon 1), Centre de Résonance Magnétique Nucléaire à Très Hauts Champs, 69100 Villeurbanne, France. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland. j.r.lewandowski@warwick.ac.uk martin.blackledge@ibs.fr lyndon.emsley@epfl.ch.
  • 2015-05-02
Published in:
  • Science (New York, N.Y.). - 2015
Molecular Dynamics Simulation
Motion
Nanoparticles
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Solvents
Water
English 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.
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  • English
Open access status
green
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https://sonar.ch/global/documents/99709
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