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

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.
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Nature Communications, Nature Publishing Group, 2015, 6, pp.6490
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http://hal.univ-grenoble-alpes.fr/hal-01162282
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Soumis le : mercredi 10 juin 2015 - 09:44:16
Dernière modification le : lundi 19 février 2018 - 14:34:03

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Giorgio Schirò, Yann Fichou, Francois-Xavier Gallat, Kathleen Wood, Frank Gabel, et al.. Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins.. Nature Communications, Nature Publishing Group, 2015, 6, pp.6490. 〈hal-01162282〉

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