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Nat Commun. 2015 Mar 16;6:6490. doi: 10.1038/ncomms7490.

Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins.

Author information

1
1] IBS, Univ. Grenoble Alpes, IBS, F-38044 Grenoble, France [2] CNRS, IBS, 71 avenue des Martyrs, F-38044 Grenoble, France [3] CEA, IBS, F-38044 Grenoble, France.
2
1] IBS, Univ. Grenoble Alpes, IBS, F-38044 Grenoble, France [2] CNRS, IBS, 71 avenue des Martyrs, F-38044 Grenoble, France [3] CEA, IBS, F-38044 Grenoble, France [4] Department of Chemistry, University of California, Irvine, California 92697-2025, USA.
3
1] IBS, Univ. Grenoble Alpes, IBS, F-38044 Grenoble, France [2] CNRS, IBS, 71 avenue des Martyrs, F-38044 Grenoble, France [3] CEA, IBS, F-38044 Grenoble, France [4] Institut Laue-Langevin, 71 avenue des Martyrs, 38000 Grenoble, France.
4
Australian Nuclear Science and Technology Organisation Bragg Institute, Menai, New Illawarra Road, Lucas Heights, NSW 2234, Australia.
5
1] Institut Laue-Langevin, 71 avenue des Martyrs, 38000 Grenoble, France [2] ILL-EMBL Deuteration Laboratory, Partnership for Structural Biology, 38044 Grenoble, France.
6
Max-Planck-Institut für Kohlenforschung, 45470 Mülheim an der Ruhr, Germany.
7
Dipartimento di Fisica e Geologia, Università di Perugia, Via Pascoli, 06123 Perugia, Italy.
8
Forschungszentrum Jülich, JCNS at MLZ, Lichtenbergstrasse 1, 85747 Garching, Germany.
9
Department of Chemistry, University of California, Irvine, California 92697-2025, USA.

Abstract

Hydration water is the natural matrix of biological macromolecules and is essential for their activity in cells. The coupling between water and protein dynamics has been intensively studied, yet it remains controversial. Here we combine protein perdeuteration, neutron scattering and molecular dynamics simulations to explore the nature of hydration water motions at temperatures between 200 and 300 K, across the so-called protein dynamical transition, in the intrinsically disordered human protein tau and the globular maltose binding protein. Quasi-elastic broadening is fitted with a model of translating, rotating and immobile water molecules. In both experiment and simulation, the translational component markedly increases at the protein dynamical transition (around 240 K), regardless of whether the protein is intrinsically disordered or folded. Thus, we generalize the notion that the translational diffusion of water molecules on a protein surface promotes the large-amplitude motions of proteins that are required for their biological activity.

PMID:
25774711
PMCID:
PMC4382692
DOI:
10.1038/ncomms7490
[Indexed for MEDLINE]
Free PMC Article

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