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Related Concept Videos

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 Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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 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,...

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Related Experiment Video

Updated: Jul 2, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

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

Published on: November 12, 2012

Protein complex evolution does not involve extensive network rewiring.

Teunis J P van Dam1, Berend Snel

  • 1Theoretical Biology and Bioinformatics Group, Department of Biology, Utrecht University, Utrecht, The Netherlands.

Plos Computational Biology
|August 20, 2008
PubMed
Summary
This summary is machine-generated.

Protein complex membership is highly conserved across species, with evolution primarily driven by gene gain or loss rather than network rewiring. This study leverages new high-throughput data to assess evolutionary dynamics of protein interactions.

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Last Updated: Jul 2, 2026

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

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

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Systems Biology

Background:

  • Protein complexes are essential for cellular function.
  • Understanding their evolution is crucial but limited by data on high-throughput (HTP) interactome technologies.

Purpose of the Study:

  • To assess the evolutionary conservation of protein complex membership.
  • To investigate the drivers of protein complex evolution using new HTP data.

Main Methods:

  • Comparative genomics between human curated complexes and HTP protein co-purification data in yeast (Saccharomyces cerevisiae).
  • Analysis of ortholog presence/absence to determine conservation of protein pair co-complex membership.

Main Results:

  • New yeast HTP datasets show lower false negative rates, enabling better conservation estimates.
  • 90% of human protein complex pairs with conserved genes show conserved co-complex membership in yeast.
  • Disruption of co-complex membership is mainly due to gene loss/gain, not network rewiring.

Conclusions:

  • Protein complex evolution is predominantly shaped by gene content changes.
  • Genomic evolution and protein interaction network evolution are tightly linked.
  • New HTP interactome data significantly improves the study of protein complex evolution.