Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPrinciples of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?Ozlem Keskin, Attila Gursoy, Buyong Ma, and Ruth NussinovView Author Information Koc University, Center for Computational Biology and Bioinformatics and College of Engineering, Rumelifeneri Yolu, 34450 Sariyer Istanbul, Turkey; Basic Research Program, SAIC−Frederick, Inc., Center for Cancer Research Nanobiology Program, NCIFrederick, Frederick, Maryland 21702; and Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel Cite this: Chem. Rev. 2008, 108, 4, 1225–1244Publication Date (Web):March 21, 2008Publication History Received13 July 2007Published online21 March 2008Published inissue 1 April 2008https://pubs.acs.org/doi/10.1021/cr040409xhttps://doi.org/10.1021/cr040409xresearch-articleACS PublicationsCopyright © 2008 American Chemical SocietyRequest reuse permissionsArticle Views11837Altmetric-Citations508LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Interfaces,Molecules,Peptides and proteins,Protein structure,Screening assays Get e-Alerts
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Protein-protein interfaces are characterized by hot spots or hot regions rather than even contribution across all contact areas.
“Protein-protein interfaces are characterized by the existence of hot spots or ‘hot regions’ in interacting regions instead of an even contribution across all contact areas.371,476,487,492–495”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [476]
The same physical forces that drive protein folding are also responsible for protein-protein associations.
“The same physical forces that drive protein folding are also responsible for protein-protein associations5.”
From AF2Complex predicts direct physical interactions in multimeric proteins with deep learning (2022) · cites this paper as [5]
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- Authors
- Keskin, O., Gursoy, A., Ma, B., & Nussinov, R.
- Affiliations
- Koc University, Center for Computational Biology and Bioinformatics and College of Engineering, Rumelifeneri Yolu, 34450 Sariyer Istanbul, Turkey; Basic Research Program, SAIC−Frederick, Inc., Center for Cancer Research Nanobiology Program, NCIFrederick, Frederick, Maryland 21702; and Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel
- Koç University (TR)
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-03-21
- Volume
- 108
- Issue
- 4
- Pages
- 1225-1244
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2087574732
- Cited by
- 697
- References
- 225
- Citations by year
- 2026: 32 · 2025: 44 · 2024: 42 · 2023: 37 · 2022: 40 · 2021: 40 · 2020: 33 · 2019: 38 · 2018: 49 · 2017: 33 · 2016: 33 · 2015: 41 · 2014: 36 · 2013: 42 · 2012: 36
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (n01co12400-79-0-22)
- National Cancer Institute (N01CO12400)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- protein-protein interaction, interaction interfaces, binding free energy, binding affinity, protein folding, protein stability, protein engineering, protein solubility, protein misfolding, protein refolding, protein folding kinetics, protein folding thermodynamics, protein folding pathways, folding intermediates
- MeSH terms
- Allosteric Regulation, Binding Sites, Models, Molecular, Protein Binding, Protein Conformation, Proteins
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