Hydration, slaving and protein function

Hydration, slaving and protein function
复制标题

DOI:
10.1016/s0301-4622(02)00083-2
复制
发表时间:
2002-07-10
影响因子:
3.8
通讯作者:
McMahon, BH
McMahon, BH
中科院分区:
生物学4区
文献类型:
--
作者:
Frauenfelder, H;Fenimore, PW;McMahon, BH

文献摘要

被引文献

相似文献

蛋白质动力学对蛋白质功能起着至关重要的作用。生命系统中的蛋白质并不是孤立的,而是在网络和严格监管的环境中运行。因此,了解蛋白质动力学的外部控制是重要的。水合作用和溶剂粘度是环境的显著特性。脱水的蛋白质和在僵硬环境中的蛋白质不能正常工作。因此,必须详细了解水合作用和溶剂粘度的影响。我们讨论了分离这两种效应的实验。这些实验主要是用野马和抹香鲸的肌红蛋白进行的,使用广泛温度范围内一氧化碳的结合作为工具。实验表明,仅在生理温度范围内获取的数据不足以理解水化和溶剂对蛋白质松弛和功能的影响。虽然实际数据来自肌红蛋白,但预计结果适用于大多数或所有球状蛋白。(C)2002 Elsevier Science B.V.保留所有权利。
Protein dynamics is crucial for protein function. Proteins in living systems are not isolated, but operate in networks and in a carefully regulated environment. Understanding the external control of protein dynamics is consequently important. Hydration and solvent viscosity are among the salient properties of the environment. Dehydrated proteins and proteins in a rigid environment do not function properly. It is consequently important to understand the effect of hydration and solvent viscosity in detail. We discuss experiments that separate the two effects. These experiments have predominantly been performed with wild-type horse and sperm whale myoglobin, using the binding of carbon monoxide over a broad range of temperatures as a tool. The experiments demonstrate that data taken only in the physiological temperature range are not sufficient to understand the effect of hydration and solvent on protein relaxation and function. While the actual data come from myoglobin, it is expected that the results apply to most or all globular proteins. (C) 2002 Elsevier Science B.V. All rights reserved.