TY  - JOUR
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
TI  - Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins
JO  - Nature Communications
VL  - 6
SN  - 2041-1723
CY  - London
PB  - Nature Publishing Group
M1  - FZJ-2015-02214
SP  - 6490
PY  - 2015
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 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000352719300003
C6  - pmid:25774711
DO  - DOI:10.1038/ncomms7490
UR  - https://juser.fz-juelich.de/record/188918
ER  -