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Related Experiment Video

Updated: Feb 2, 2026

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

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

Published on: April 1, 2017

Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry.

Dror S Chorev¹, Lindsay A Baker², Di Wu¹

¹Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.

Science (New York, N.Y.)

|November 17, 2018

Summary

Researchers developed a new method to study intact membrane protein assemblies without chemical disruption. This technique preserves native interactions and functions, offering deeper insights into cellular processes.

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Last Updated: Feb 2, 2026

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

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Published on: April 1, 2017

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

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Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Membrane proteins are crucial for cellular functions but are difficult to study due to their lipid bilayer environment.
Traditional extraction methods often disrupt protein complexes and their native interactions.
Understanding membrane protein integrity is key to elucidating cellular mechanisms.

Purpose of the Study:

To develop a non-disruptive method for isolating intact membrane protein assemblies.
To characterize the composition and interactions of native membrane protein complexes using mass spectrometry.
To investigate the importance of the native membrane environment for protein function and stability.

Main Methods:

Developed a novel technique to eject intact membrane protein assemblies from lipid bilayers without chemical lysis.
Utilized mass spectrometry to analyze the composition of the ejected assemblies.
Applied the method to both bacterial (Escherichia coli) and eukaryotic (Bos taurus) membranes.

Main Results:

Successfully identified intact chaperone-porin complexes and lipid interactions within the beta-barrel assembly machinery in E. coli.
Observed efflux pumps spanning bacterial inner and outer membranes.
Characterized the pentameric TonB pore and the SecYEG channel associated with ATP synthase in E. coli inner membranes.
Isolated respiratory complexes and ADP/ATP translocase dimers bound to fatty acids from Bos taurus mitochondria.

Conclusions:

The non-disruptive isolation method preserves native protein-protein and protein-lipid interactions.
The native membrane environment is critical for maintaining small-molecule binding, subunit associations, and chaperone interactions.
This approach provides a powerful tool for studying the native membrane proteome and its functional complexes.