Issue 32, 2008
From the journal:

Physical Chemistry Chemical Physics

Hydration water rotational motion as a source of configurational entropy driving protein dynamics. Crossovers at 150 and 220 K

J.-M. Zanotti,*a   G. Gibrat†a  and  M.-C. Bellissent-Funelb  

* Corresponding authors

a CEA, IRAMIS, Laboratoire Léon Brillouin, CEA Saclay, Gif-sur-Yvette, France
E-mail: jmzanotti@cea.fr

b CNRS, Laboratoire Léon Brillouin, CEA Saclay, Gif-sur-Yvette, France

Abstract

The existence of a protein dynamic transition around 220 K is widely known and the central role of the protein hydration shell is now largely recognized as the driving force for this transition. In this paper, we propose a mechanism, at the molecular level, for the contribution of hydration water. In particular, we identify the key importance of rotational motion of the hydration water as a source of configurational entropy triggering (i) the 220 K protein dynamic crossover (the so-called dynamic transition) but also (ii) a much less intense and scarcely reported protein dynamic crossover, associated to a calorimetric glass transition, at 150 K.

Graphical abstract: Hydration water rotational motion as a source of configurational entropy driving protein dynamics. Crossovers at 150 and 220 K

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Article information

DOI
https://doi.org/10.1039/B808217K
Article type
Paper
Submitted
14 May 2008
Accepted
02 Jul 2008
First published
16 Jul 2008

Phys. Chem. Chem. Phys., 2008,10, 4865-4870

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Hydration water rotational motion as a source of configurational entropy driving protein dynamics. Crossovers at 150 and 220 K

J.-M. Zanotti, G. Gibrat and M.-C. Bellissent-Funel, Phys. Chem. Chem. Phys., 2008, 10, 4865 DOI: 10.1039/B808217K

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