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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 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-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...
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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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...

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Related Experiment Video

Updated: Jul 2, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

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

Published on: March 3, 2015

Evolution of protein-protein interaction network.

T Makino1, T Gojobori

  • 1Center for Information Biology and DNA Data Bank of Japan, National Institute of Genetics, Yata, Mishima, Japan.

Genome Dynamics
|August 30, 2008
PubMed
Summary

The evolutionary rates of proteins involved in protein-protein interactions (PPIs) are significantly influenced by their interaction partners. Understanding these PPIs is crucial for comprehending biological network evolution and organism diversification.

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Related Experiment Videos

Last Updated: Jul 2, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

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

Published on: March 3, 2015

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Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Area of Science:

  • Evolutionary biology
  • Systems biology
  • Bioinformatics

Background:

  • Protein-protein interactions (PPIs) are fundamental to biological networks.
  • The number of PPIs a protein engages in influences its evolutionary rate.
  • Understanding PPI evolution is key to explaining organismal diversification.

Purpose of the Study:

  • To investigate the evolutionary rates of proteins involved in PPIs.
  • To analyze how PPI characteristics affect protein evolutionary rates.
  • To review the current understanding of duplicated gene products in PPI networks.

Main Methods:

  • Analysis of evolutionary rates of proteins within PPI networks.
  • Examination of duplicated gene products involved in PPIs.
  • Assessment of characteristic features of PPIs and their influence on protein evolution.

Main Results:

  • The evolutionary rates of proteins in PPI networks are strongly dictated by their interaction partners.
  • Specific features of PPIs significantly influence the evolutionary trajectory of associated proteins.

Conclusions:

  • Evolutionary dynamics of proteins are intrinsically linked to their PPI partners.
  • Considering the evolution of PPI proteins is essential for understanding the construction of current PPI networks.
  • This research highlights the importance of PPI network evolution in shaping biological complexity.