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Related Concept Videos

Protein Networks02:26

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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein-protein Interfaces02:04

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 polypeptide...

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Related Experiment Video

Updated: May 19, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

A census of human soluble protein complexes.

Pierre C Havugimana1, G Traver Hart, Tamás Nepusz

  • 1Banting and Best Department of Medical Research, Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada.

Cell
|September 4, 2012
PubMed
Summary
This summary is machine-generated.

Researchers mapped 13,993 human protein interactions, revealing 622 protein complexes. Smaller complexes are less understood and appear to be more recent evolutionary innovations, offering insights into cellular processes.

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Last Updated: May 19, 2026

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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Area of Science:

  • Proteomics
  • Human biology
  • Molecular interactions

Background:

  • Cellular functions rely on stable protein associations.
  • Understanding the full network of human protein complexes is incomplete.
  • Existing knowledge gaps hinder functional and mechanistic insights.

Purpose of the Study:

  • To systematically identify physical interactions and protein complexes in human cells.
  • To create a high-confidence network of soluble human protein interactions.
  • To characterize the properties and evolutionary context of identified protein complexes.

Main Methods:

  • Utilized an integrative global proteomic profiling approach.
  • Employed chromatographic separation of cultured human cell extracts into over 1,000 fractions.
  • Analyzed fractions using quantitative tandem mass spectrometry (MS/MS).

Main Results:

  • Identified a network of 13,993 high-confidence physical interactions among 3,006 proteins.
  • Reported 622 putative protein complexes linked to core biological processes.
  • Observed that smaller complexes (≤5 subunits) are less annotated and evolutionarily restricted.

Conclusions:

  • The study provides a comprehensive map of human protein-protein interactions and complexes.
  • Smaller protein complexes represent potentially recent functional innovations.
  • Findings aid in understanding disease mechanisms and annotating uncharacterized proteins.