Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.
Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.
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DOI：
10.1021/acs.chemrev.7b00305
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发表时间：
2018-02-28
期刊：
影响因子：
62.1
通讯作者：
Pang X
中科院分区：
文献类型：
--
作者：
Zhou HX;Pang X
带电基团和极性基团通过形成离子对、氢键和其他不太具体的静电相互作用，赋予蛋白质重要的性质。氨基酸上电荷的调节，如pH值、磷酸化和去磷酸化，对蛋白质变性和信号转导网络的开关反应有重要影响。这篇综述的目的是在蛋白质电荷和极性基团的各种影响之间提出一个统一的主题。简单的模型将用于说明蛋白质中静电相互作用的基本思想，而这些思想反过来将用于阐明静电相互作用在蛋白质结构、折叠、结合、冷凝和相关生物功能中的作用。特别是，我们将研究带电侧链如何在不同类型的蛋白质中空间分布，以及静电相互作用如何影响蛋白质的热力学和动力学性质。我们的希望是捕捉重要的历史发展和最近的实验和理论进展在定量静电贡献的蛋白质。
Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less specific electrostatic interactions, impart important properties to proteins. Modulation of the charges on the amino acids, e.g., by pH and by phosphorylation and dephosphorylation, have significant effects such as protein denaturation and switch-like response of signal transduction networks. This review aims to present a unifying theme among the various effects of protein charges and polar groups. Simple models will be used to illustrate basic ideas about electrostatic interactions in proteins, and these ideas in turn will be used to elucidate the roles of electrostatic interactions in protein structure, folding, binding, condensation, and related biological functions. In particular, we will examine how charged side chains are spatially distributed in various types of proteins and how electrostatic interactions affect thermodynamic and kinetic properties of proteins. Our hope is to capture both important historical developments and recent experimental and theoretical advances in quantifying electrostatic contributions of proteins.
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