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Related Concept Videos

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 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...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: May 26, 2026

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

The evolution of multimeric protein assemblages.

Michael Lynch1

  • 1Department of Biology, Indiana University, IN, USA. milynch@indiana.edu

Molecular Biology and Evolution
|December 7, 2011
PubMed
Summary
This summary is machine-generated.

The evolution of complex cellular structures involves new protein interactions and gene duplication. This study develops a framework for understanding dimer evolution, showing its dependence on population size and the need for fitness studies.

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Last Updated: May 26, 2026

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
07:40

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Area of Science:

  • Evolutionary biology
  • Molecular evolution
  • Population genetics

Background:

  • Complex cellular features arise from evolutionary processes.
  • New protein-protein interactions and gene duplication are key mechanisms.
  • Understanding the evolution of protein complexes remains a challenge.

Purpose of the Study:

  • To develop a theoretical framework for understanding the evolution of protein dimers.
  • To identify factors influencing the evolutionary pathways of protein complex emergence.

Main Methods:

  • Utilized data on protein multimerization levels across major phylogenetic groups.
  • Applied population-genetic theory to assess the plausibility of evolutionary pathways.
  • Developed a framework to explain the emergence of protein dimers.

Main Results:

  • The likelihood of different evolutionary pathways for protein complex formation is strongly dependent on effective population size.
  • A theoretical framework for dimer evolution has been established.

Conclusions:

  • Effective population size is a critical factor in the evolution of protein complexes.
  • Future research should focus on comparative studies of monomeric and dimeric protein fitness consequences to advance understanding.