Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 10, Issue 32, Pages 4865-4870Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b808217k
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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.
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