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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-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...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
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...

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Related Experiment Video

Updated: May 16, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Photocrosslinking approaches to interactome mapping.

Nam D Pham1, Randy B Parker, Jennifer J Kohler

  • 1Department of Biochemistry, 5323 Harry Hines Boulevard, University of Texas Southwestern Medical Center, Dallas, TX 75390-9038, USA.

Current Opinion in Chemical Biology
|November 15, 2012
PubMed
Summary
This summary is machine-generated.

Cell-based photocrosslinking maps protein interactions in living cells. This method reveals context-dependent interactions, dynamics, and transient protein engagements for various cellular processes.

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Mapping Dysfunctional Protein-Protein Interactions in Disease

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Last Updated: May 16, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Area of Science:

  • Cellular biology
  • Biochemistry
  • Molecular interactions

Background:

  • Mapping cellular interactomes is crucial for understanding biological processes.
  • Existing methods may not capture context-dependent or transient interactions within living cells.

Purpose of the Study:

  • To discuss the application of cell-based photocrosslinking for mapping interactome networks.
  • To highlight the advantages of photocrosslinking in native cellular environments.

Main Methods:

  • Incorporating photocrosslinking analogs of amino acids or sugars into cellular biomolecules via metabolic engineering or genetic code expansion.
  • Utilizing immunological and mass spectrometry techniques to analyze crosslinked complexes.

Main Results:

  • Photocrosslinking enables the study of context-dependent interactions in native cellular settings.
  • This technique is effective for determining interactome dynamics, mapping interaction interfaces, and identifying transient interactions.
  • Applications include immune cell signaling, transcription, membrane protein dynamics, nucleocytoplasmic transport, and protein folding.

Conclusions:

  • Cell-based photocrosslinking is a powerful tool for dissecting complex cellular interactomes.
  • It provides insights into dynamic and transient protein interactions crucial for cellular function.
  • The method offers a versatile approach to studying diverse biological problems.