Ligand Binding, Protein Fluctuations, And Allosteric Free Energy

M. Wall
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引用次数: 7

Abstract

Although the importance of protein dynamics in protein function is generally recognized, the role of protein fluctuations in allosteric effects scarcely has been considered. To address this gap, the Kullback‐Leibler divergence (Dx) between protein conformational distributions before and after ligand binding was proposed as a means of quantifying allosteric effects in proteins. Here, previous applications of Dx to methods for analysis and simulation of proteins are first reviewed, and their implications for understanding aspects of protein function and protein evolution are discussed. Next, equations for Dx suggest that kBTDx should be interpreted as an allosteric free energy — the free energy associated with changing the ligand‐free protein conformational distribution to the ligand‐bound conformational distribution. This interpretation leads to a thermodynamic model of allosteric transitions that unifies existing perspectives on the relation between ligand binding and changes in protein conformational dis...
配体结合、蛋白质波动和变构自由能
虽然蛋白质动力学在蛋白质功能中的重要性已得到普遍认识,但蛋白质波动在变构效应中的作用却很少被考虑。为了解决这一差距,提出了配体结合前后蛋白质构象分布之间的Kullback - Leibler散度(Dx)作为定量蛋白质变构效应的一种手段。本文首先回顾了Dx在蛋白质分析和模拟方法中的应用,并讨论了它们对理解蛋白质功能和蛋白质进化方面的意义。接下来,Dx的方程表明,kBTDx应该被解释为一种变构自由能——将无配体的蛋白质构象分布改变为配体结合的构象分布的自由能。这种解释导致了变构转变的热力学模型,该模型统一了关于配体结合与蛋白质构象变化之间关系的现有观点。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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