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

被引:49
作者
Zanotti, J. -M. [1 ]
Gibrat, G. [1 ]
Bellissent-Funel, M. -C. [2 ]
机构
[1] CEA Saclay, CEA, IRAMIS, Lab Leon Brillouin, F-91191 Gif Sur Yvette, France
[2] CEA Saclay, Lab Le Brillouin, CNRS, F-91191 Gif Sur Yvette, France
关键词
D O I
10.1039/b808217k
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
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.
引用
收藏
页码:4865 / 4870
页数:6
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