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Related Experiment Video

Updated: Jun 6, 2026

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

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

Reeling in the catch: advancing cleavable linkers for proteomics.

Meng M Rowland¹, Michael D Best

¹Department of Chemistry, The University of Tennessee, 1420 Circle Drive, Knoxville, TN 37996, USA.

Chemistry & Biology

|November 25, 2010

Summary

Researchers developed a novel diazobenzene-cleavable linker system to improve protein purification in bioorthogonal chemistry applications. This breakthrough aids in the effective release of labeled proteins for global proteomic studies.

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

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Published on: July 14, 2015

Area of Science:

Biochemistry
Chemical Biology
Proteomics

Background:

Global proteomic studies often involve derivatizing proteins using bioorthogonal chemistry.
A significant challenge in these applications is the efficient release of purified, labeled proteins from solid supports.

Discussion:

This study investigates the utility of a diazobenzene-cleavable linker system for addressing the protein release challenge.
The diazobenzene linker offers a chemical strategy for controlled cleavage and liberation of tagged proteins.

Key Insights:

The diazobenzene-cleavable linker system demonstrates effectiveness in facilitating the release of derivatized proteins.
This method provides a robust solution for sample preparation in complex proteomic workflows.
Successful implementation enables more accurate protein characterization and analysis.

Outlook:

Further optimization of linker chemistry could enhance compatibility with diverse bioorthogonal reactions.
This approach holds potential for advancing high-throughput proteomic analyses.
The developed system may find applications in other areas requiring controlled release of biomolecules.