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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...
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...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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...

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Related Experiment Video

Updated: Jun 21, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Evolutionary flexibility of protein complexes.

Michael F Seidl1, Jörg Schultz

  • 1Department of Bioinformatics, Biozentrum, University Würzburg, Am Hubland, 97074 Würzburg, Germany.

BMC Evolutionary Biology
|July 9, 2009
PubMed
Summary
This summary is machine-generated.

Protein complex evolution is flexible, with frequent component additions and losses across species. This dynamic process, unlike random gene changes, shapes protein complexes, revealing evolutionary cores.

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Area of Science:

  • Proteomics and Evolutionary Biology
  • Systems Biology
  • Bioinformatics

Background:

  • Proteins function within dynamic complexes, crucial for cellular processes.
  • Complex composition changes through component additions and losses, impacting evolution.
  • Previous studies suggested this flexibility is limited to specific complexes.

Purpose of the Study:

  • To investigate the prevalence of flexible evolution in protein complexes on a large scale.
  • To determine if component additions/losses are a general trend or limited to a few complexes.

Main Methods:

  • Analysis of a manually curated human protein complex dataset (HPRD).
  • Computation of interologs across 25 species to predict complex composition.
  • Comparison of observed evolutionary patterns against random models.

Main Results:

  • Most human protein complexes exhibit high compositional flexibility across species.
  • Only 25% of genes remained unchanged; 75% of complexes experienced component loss.
  • Evolutionary patterns significantly deviated from random gene models, with rare whole complex loss.

Conclusions:

  • Component additions and losses are fundamental to protein complex evolution.
  • Evolutionary dynamics of protein complexes differ significantly from random gene evolution.
  • Taxon-specific changes may relate to cellular or morphological adaptations, highlighting evolutionary cores.