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Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

Protein-Protein Interfaces

Protein-Protein Interfaces

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Protein Networks

Protein Networks

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

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Related Experiment Video

Updated: Mar 21, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Published on: March 3, 2015

Recent advances in large-scale protein interactome mapping.

Virja Mehta¹, Laura Trinkle-Mulcahy¹

¹Department of Cellular and Molecular Medicine, Ottawa Institute of Systems Biology, University of Ottawa, Ottawa, ON, Canada.

|May 10, 2016

Summary

This summary is machine-generated.

Mapping protein-protein interactions (PPIs) is crucial for understanding cellular functions. Recent advancements in computational prediction, literature curation, and high-throughput experimental strategies are improving the comprehensive mapping of these complex biological networks.

Keywords:

AP-MS APEX BioID Interactome PCP Proteomics XL-MS affinity purification-mass spectrometry cross-linking MS analysis protein correlation profiling

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

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Mapping Dysfunctional Protein-Protein Interactions in Disease

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Published on: October 24, 2025

Area of Science:

Molecular Biology
Systems Biology
Bioinformatics

Background:

Protein-protein interactions (PPIs) are fundamental to cellular processes.
Comprehensive mapping of PPI networks is essential for systems biology and focused research.
Significant challenges exist in mapping the complete spectrum of protein interactions.

Purpose of the Study:

To highlight recent advancements in mapping protein-protein interaction networks.
To emphasize the integration of computational and experimental approaches.
To underscore the importance of public databases for PPI data.

Main Methods:

Computational prediction of protein-protein interactions.
Literature curation of low-throughput studies on protein complexes.
High-throughput experimental strategies for mapping PPIs.
Deposition of data into public databases.

Main Results:

Improvements in computational prediction accuracy for PPIs.
Enhanced literature curation yields valuable low-throughput interaction data.
Increased availability of high-quality, non-biased high-throughput PPI data.
Growing repositories of PPI information in public databases.

Conclusions:

Major strides have been made in mapping protein-protein interaction networks.
The combination of diverse methodologies is accelerating PPI discovery.
Publicly accessible, high-quality data is crucial for advancing systems biology and biological research.