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

Giorgio Schirò (), Yann Fichou, Francois-Xavier Gallat, Kathleen Wood, Frank Gabel, Martine Moulin, Michael Härtlein, Matthias Heyden, Jacques-Philippe Colletier, Andrea Orecchini, Alessandro Paciaroni, Joachim Wuttke, Douglas J. Tobias () and Martin Weik ()
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Giorgio Schirò: IBS, Univ. Grenoble Alpes, IBS
Yann Fichou: IBS, Univ. Grenoble Alpes, IBS
Francois-Xavier Gallat: IBS, Univ. Grenoble Alpes, IBS
Kathleen Wood: Australian Nuclear Science and Technology Organisation Bragg Institute
Frank Gabel: IBS, Univ. Grenoble Alpes, IBS
Martine Moulin: Institut Laue-Langevin
Michael Härtlein: Institut Laue-Langevin
Matthias Heyden: Max-Planck-Institut für Kohlenforschung
Jacques-Philippe Colletier: IBS, Univ. Grenoble Alpes, IBS
Andrea Orecchini: Università di Perugia, Via Pascoli
Alessandro Paciaroni: Università di Perugia, Via Pascoli
Joachim Wuttke: Forschungszentrum Jülich, JCNS at MLZ
Douglas J. Tobias: University of California
Martin Weik: IBS, Univ. Grenoble Alpes, IBS

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms7490

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