TY - JOUR
T1 - Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins
AU - Schirò, Giorgio
AU - Fichou, Yann
AU - Gallat, Francois Xavier
AU - Wood, Kathleen
AU - Gabel, Frank
AU - Moulin, Martine
AU - Härtlein, Michael
AU - Heyden, Matthias
AU - Colletier, Jacques Philippe
AU - Orecchini, Andrea
AU - Paciaroni, Alessandro
AU - Wuttke, Joachim
AU - Tobias, Douglas J.
AU - Weik, Martin
N1 - Funding Information:
We are grateful to Giuseppe Zaccai for continuous and fruitful discussions on the relationship between protein and water dynamics. Martin Blackledge is acknowledged for having provided tau conformations for MD simulations before publication. Financial support by the CEA, the CNRS and the UJF is acknowledged, as well as a grant from the Agence Nationale de la Recherche (project number ANR-11-BSV5-027) to M.W. This work has benefited from the activities of the DLAB consortium funded by the EU under contracts HPRI-2001-50065 and RII3-CT-2003-505925, and from UK EPSRC-funded activity within the ILL-EMBL Deuteration Laboratory under grants GR/R99393/ 01 and EP/C015452/1. The study has been supported by the European Commission under the 7th Framework Programme through the ’Research Infrastructures’ action of the ’Capacities’ Programme, Contract No: CP-CSA_INFRA-2008-1.1.1 Number 226507-NMI3. M. Heyden gratefully acknowledges financial support from the German Academy of Sciences Leopoldina (LPDS 2011-4). Y.F. is grateful to the Fulbright Scholar Program, which provided support for his visit to UC Irvine, to carry out the MD simulations. K.W. acknowledges funding from the access to major research facilities programme, supported by the Commonwealth of Australia under the International Science Linkages program.
Publisher Copyright:
© 2015 Macmillan Publishers Limited. All rights reserved.
PY - 2015/3/16
Y1 - 2015/3/16
N2 - 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.
AB - 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.
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U2 - 10.1038/ncomms7490
DO - 10.1038/ncomms7490
M3 - Article
C2 - 25774711
AN - SCOPUS:84928819941
SN - 2041-1723
VL - 6
JO - Nature communications
JF - Nature communications
M1 - 6490
ER -