This title appears in the Scientific Report :
2015
Please use the identifier:
http://dx.doi.org/10.1038/ncomms7490 in citations.
Please use the identifier: http://hdl.handle.net/2128/8463 in citations.
Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins
Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins
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 dyna...
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Personal Name(s): | Schirò, Giorgio (Corresponding Author) |
---|---|
Fichou, Yann / Gallat, Francois-Xavier / Wood, Kathleen / Gabel, Frank / Moulin, Martine / Härtlein, Michael / Heyden, Matthias / Colletier, Jacques-Philippe / Orecchini, Andrea / Paciaroni, Alessandro / Wuttke, Joachim / Tobias, Douglas J. (Corresponding Author) / Weik, Martin (Corresponding Author) | |
Contributing Institute: |
Streumethoden; JCNS-2 Neutronenstreuung; JCNS-1 JCNS-FRM-II; JCNS-FRM-II |
Published in: | Nature Communications, 6 (2015) S. 6490 |
Imprint: |
London
Nature Publishing Group
2015
|
DOI: |
10.1038/ncomms7490 |
PubMed ID: |
25774711 |
Document Type: |
Journal Article |
Research Program: |
Jülich Centre for Neutron Research (JCNS) FRM II / MLZ |
Subject (ZB): | |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/8463 in citations.
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. |