Department of Chemistry and Department of Physics, University of Illinois at Chicago , Chicago, Illinois 60607, United States.
Department of Physics and Institute of Molecular Biophysics, Florida State University , Tallahassee, Florida 32306, United States.
Chem Rev. 2018 Feb 28;118(4):1691-1741. doi: 10.1021/acs.chemrev.7b00305. Epub 2018 Jan 10.
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.
带电基团和极性基团通过形成离子对、氢键和其他非特异性静电相互作用，赋予蛋白质重要的性质。氨基酸上电荷的调节，例如通过 pH 值以及磷酸化和去磷酸化，会产生显著的影响，如蛋白质变性和信号转导网络的类似开关的响应。本综述旨在提出蛋白质电荷和极性基团的各种作用之间的统一主题。将使用简单的模型来说明蛋白质中静电相互作用的基本概念，而这些概念反过来又将用于阐明静电相互作用在蛋白质结构、折叠、结合、凝聚和相关生物学功能中的作用。特别是，我们将研究各种类型的蛋白质中带电荷的侧链是如何在空间上分布的，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。我们希望既能捕捉到蛋白质静电作用定量研究的重要历史发展，也能捕捉到最近的实验和理论进展。
