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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...
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...
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...

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Related Experiment Video

Updated: May 9, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
10:37

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

Protein complexes: breaking up is hard to do well.

Rachel R Ogorzalek Loo1, Joseph A Loo

  • 1Department of Biological Chemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Structure (London, England : 1993)
|August 13, 2013
PubMed
Summary

Mass spectrometry can determine protein assembly size and stoichiometry. Gas-phase dissociations accurately reflect solution structures for specific protein complex types.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Mass Spectrometry

Background:

  • Mass spectrometry (MS) is a powerful analytical technique for characterizing biomolecules.
  • Understanding the structure of protein assemblies is crucial for deciphering their biological functions.
  • Previous methods for studying protein complexes in the gas phase had limitations in recapitulating solution structures.

Purpose of the Study:

  • To investigate whether gas-phase dissociations of protein assemblies can accurately reflect their structures in solution.
  • To identify the characteristics of protein complexes that enable successful structure recapitulation via gas-phase methods.

Main Methods:

  • Utilizing mass spectrometry to analyze protein assemblies.
  • Performing gas-phase dissociations on selected protein complexes.

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

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Related Experiment Videos

Last Updated: May 9, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
10:37

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

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

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

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

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  • Comparing gas-phase structural data with known solution-state structures.

    • Main Results:

    • Gas-phase dissociations successfully recapitulated solution structures for certain protein assemblies.
    • Recapitulation of solution structure was observed for complexes with specific properties:
    • These properties include few intersubunit salt bridges, high charge density, inflexible subunits, or small intersubunit interfaces.

    Conclusions:

    • Gas-phase mass spectrometry is a viable method for studying the structure of protein assemblies.
    • The success of this method is dependent on the specific characteristics of the protein complex.
    • This approach offers new insights into protein complex organization and dynamics.