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Related Experiment Video

Updated: May 8, 2026

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

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

Published on: March 9, 2010

Novel methods for studying multiprotein complexes in vivo.

Virja Mehta¹, Laura Trinkle-Mulcahy

¹Department of Cellular and Molecular Medicine, Ottawa Institute of Systems Biology, University of Ottawa 451 Smyth Road, Ottawa, ON K1H 8M5 Canada.

F1000Prime Reports

|August 23, 2013

Summary

This summary is machine-generated.

Understanding protein complexes is key to cell function. This review highlights advanced methods for mapping these protein interactions in vivo, improving resolution and revealing cellular organization.

More Related Videos

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

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

Published on: May 5, 2017

Related Experiment Videos

Last Updated: May 8, 2026

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

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

Published on: March 9, 2010

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

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

Published on: May 5, 2017

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Proteins function in complexes (homo- and heteromeric) to perform cellular tasks.
Studying protein-protein interactions is crucial for understanding cellular organization.
Previous methods lacked sufficient spatiotemporal resolution.

Purpose of the Study:

To review novel techniques for analyzing in vivo protein complexes.
To highlight advances in structural, functional, and temporal resolution of protein interactions.

Main Methods:

Proximity-dependent labeling
Cross-linking/mass spectrometry
Pulse-chase epitope labeling
Targeted protein degradation

Main Results:

Recent advances significantly improve the analysis of in vivo complexes.
Novel approaches offer enhanced structural, functional, and temporal resolution.
These techniques enable detailed mapping of modular functional units within cells.

Conclusions:

Advanced methods are revolutionizing the study of protein complexes.
Improved resolution facilitates a deeper understanding of cellular processes.
This review provides insights into cutting-edge techniques for protein interaction analysis.