Evidence map›Paper›PMID 29319301›Full record

ReviewChemical reviews2018

Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.

Huan-Xiang Zhou, Xiaodong Pang

Abstract readReview
In one paragraph

Review in Chemical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 404 papers.

0numbers the graph read from it
0cells of the map it votes in
404citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

404 citing papers in PubMed.

  1. Article
  2. Article
  3. Metabolic Structure: A Paradigm Revisited in Light of the Fundamental Parameters of Living Systems.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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  15. Article
  16. Article
  17. Review
  18. Article
  19. Development of an HInternational journal of molecular sciences · 2026
    Article
  20. Article

344 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Huan-Xiang ZhouDepartment of Chemistry and Department of Physics, University of Illinois at Chicago , Chicago, Illinois 60607, United States.ORCID 0000-0001-9020-0302
Xiaodong PangDepartment of Physics and Institute of Molecular Biophysics, Florida State University , Tallahassee, Florida 32306, United States.

Funding

Quantitative, Mechanistic Studies of Biomolecular RecognitionR35GM118091 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI Huan-Xiang Zhou · 2016 to 2026
$6.5M
THEORY OF PROTEIN/PROTEIN ASSOCIATIONR01GM058187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 1998 to 2016
$3.7M
Modeling Crowding and Confinement of Cellular EnvironmentsR01GM088187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 2010 to 2015
$1.6M
NIGMS NIH HHS R01 GM058187NIGMS NIH HHS R01 GM088187NIGMS NIH HHS R35 GM118091
6 · The paper itself

Abstract

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.

Indexed as

Static ElectricityKineticsProtein BindingProtein ConformationProtein FoldingProteinsThermodynamicsProteins

Identifiers

PMID29319301
PMCPMC5831536

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.