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, Martin Weik

Research output: Contribution to journalArticlepeer-review

154 Scopus citations

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 300K, 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 translationa component markedly increases at the protein dynamical transition (around 240K), 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.

Original languageEnglish (US)
Article number6490
JournalNature communications
Volume6
DOIs
StatePublished - Mar 16 2015
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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