The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation
Open accessAbstract
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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Cites
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Metadata
- Authors
- Zhou, H.-X., & Pang, X.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-01-10
- Volume
- 118
- Issue
- 4
- Pages
- 1691-1741
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2783855936
- Cited by
- 1,190
- References
- 22
- FWCI
- 5.87
- Type
- journal article
- Language
- en
- Open access
- green
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