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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 Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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.
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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Disruption of protein complexes.

Golnaz Taheri1, Mahnaz Habibi, Limsoon Wong

  • 1School of Mathematics and Computer Sciences, College of Science, University of Tehran, Tehran, Iran.

Journal of Bioinformatics and Computational Biology
|June 26, 2013
PubMed
Summary
This summary is machine-generated.

Identifying key proteins is crucial for understanding biological functions. A new spectral bipartitioning method efficiently finds minimal protein sets that, when removed, maximally disrupt yeast protein complexes, revealing essential biological roles.

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Last Updated: May 10, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

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Studying Protein Function and the Role of Altered Protein Expression by Antibody Interference and Three-dimensional Reconstructions
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Studying Protein Function and the Role of Altered Protein Expression by Antibody Interference and Three-dimensional Reconstructions

Published on: April 21, 2016

Area of Science:

  • Molecular Biology
  • Systems Biology
  • Bioinformatics

Background:

  • Protein complexes are vital molecular machines essential for biological processes.
  • Disruption of protein complexes can lead to severe cellular dysfunction or organism lethality.
  • Identifying critical proteins is key to understanding complex stability and function.

Purpose of the Study:

  • To develop a method for identifying a minimal set of proteins whose removal maximally disrupts protein complexes.
  • To understand the biological significance of these identified proteins.
  • To compare the efficacy of this method against existing approaches.

Main Methods:

  • Application of spectral bipartitioning to identify critical proteins within a given set of protein complexes.
  • Analysis of the biological processes and functional modules associated with the identified proteins.
  • Comparison with methods based on protein connection degree and neighbor connectivity.

Main Results:

  • The spectral bipartitioning method successfully identified a minimal set of proteins.
  • Removal of these proteins caused significant disruption of yeast protein complexes, often into two near-equal, non-functional fragments.
  • The identified proteins are involved in numerous biological processes and are largely essential.
  • The method outperformed alternative strategies in identifying proteins that cause maximal complex disruption.

Conclusions:

  • Spectral bipartitioning provides an efficient and effective method for identifying critical proteins that destabilize protein complexes.
  • This approach offers a powerful tool for understanding protein complex organization and essentiality in biological systems.
  • The identified proteins represent key nodes whose removal has profound impacts on cellular machinery.