Institut de Biologie Structurale, Université Grenoble Alpes, CNRS, CEA, Grenoble, France.
J Phys Condens Matter. 2019 Nov 20;31(46):463002. doi: 10.1088/1361-648X/ab388a. Epub 2019 Aug 5.
Proteins are the molecular workhorses in a living organism. Their 3D structures are animated by a multitude of equilibrium fluctuations and specific out-of-equilibrium motions that are required for proteins to be biologically active. When studied as a function of temperature, functionally relevant dynamics are observed at and above the so-called protein dynamical transition (~240 K) in hydrated, but not in dry proteins. In this review we present and discuss the main experimental and computational results that provided evidence for the dynamical transition, with a focus on the role of hydration water dynamics in sustaining functional protein dynamics. The coupling and mutual influence of hydration water dynamics and protein dynamics are discussed and the hypotheses illustrated that have been put forward to explain the physical origin of their onsets.
蛋白质是生物体中的分子工作者。它们的三维结构受到多种平衡波动和特定非平衡运动的影响，这些波动和运动是蛋白质具有生物活性所必需的。当蛋白质在水合状态下而不是在干燥状态下，作为温度的函数进行研究时，在所谓的蛋白质动力学转变（~240K）及其以上，观察到与功能相关的动力学。在这篇综述中，我们介绍和讨论了主要的实验和计算结果，这些结果为动力学转变提供了证据，重点讨论了水合动力学在维持功能性蛋白质动力学方面的作用。讨论了水合动力学和蛋白质动力学的耦合和相互影响，并说明了为解释其起始的物理起源而提出的假设。
