Author
Listed:
- Giorgio Schirò
(IBS, Univ. Grenoble Alpes, IBS
CNRS, IBS
CEA, IBS)
- Yann Fichou
(IBS, Univ. Grenoble Alpes, IBS
CNRS, IBS
CEA, IBS
University of California)
- Francois-Xavier Gallat
(IBS, Univ. Grenoble Alpes, IBS
CNRS, IBS
CEA, IBS
Institut Laue-Langevin)
- Kathleen Wood
(Australian Nuclear Science and Technology Organisation Bragg Institute)
- Frank Gabel
(IBS, Univ. Grenoble Alpes, IBS
CNRS, IBS
CEA, IBS)
- Martine Moulin
(Institut Laue-Langevin
ILL-EMBL Deuteration Laboratory, Partnership for Structural Biology)
- Michael Härtlein
(Institut Laue-Langevin
ILL-EMBL Deuteration Laboratory, Partnership for Structural Biology)
- Matthias Heyden
(Max-Planck-Institut für Kohlenforschung)
- Jacques-Philippe Colletier
(IBS, Univ. Grenoble Alpes, IBS
CNRS, IBS
CEA, 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
CNRS, IBS
CEA, IBS)
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.
Suggested Citation
Giorgio Schirò & Yann Fichou & Francois-Xavier Gallat & Kathleen Wood & Frank Gabel & Martine Moulin & Michael Härtlein & Matthias Heyden & Jacques-Philippe Colletier & Andrea Orecchini & Alessandro P, 2015.
"Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins,"
Nature Communications, Nature, vol. 6(1), pages 1-8, May.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7490
DOI: 10.1038/ncomms7490
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Cited by:
- Köhler, Mateus Henrique & Barbosa, Rafael C. & da Silva, Leandro B. & Barbosa, Marcia C., 2017.
"Role of the hydrophobic and hydrophilic sites in the dynamic crossover of the protein-hydration water,"
Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 468(C), pages 733-739.
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