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Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation
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    Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation
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    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
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    Chemical Reviews

    Cite this: Chem. Rev. 2018, 118, 4, 1691–1741
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    https://doi.org/10.1021/acs.chemrev.7b00305
    Published January 10, 2018
    Copyright © 2018 American Chemical Society

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    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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    Cite this: Chem. Rev. 2018, 118, 4, 1691–1741
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    https://doi.org/10.1021/acs.chemrev.7b00305
    Published January 10, 2018
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