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Updated: May 25, 2026
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
Linking structural change with functional regulation-insights from mass spectrometry
Nina Morgner1, Carol V Robinson
1Department of Chemistry, University of Oxford, United Kingdom.
Current Opinion in Structural Biology
|February 4, 2012
Summary
Mass spectrometry (MS) advances reveal the functional secrets of non-covalent molecular machines. This technique helps understand cellular functions beyond just protein composition.
Area of Science:
- Biophysics
- Structural Biology
- Molecular Biology
Background:
- Understanding cellular function requires knowledge of molecular machines.
- Protein subunit identity and composition are foundational but insufficient for understanding dynamics.
- Dynamic interactions and regulatory mechanisms are key to cellular processes.
Purpose of the Study:
- To review recent developments in mass spectrometry (MS).
- To highlight MS applications in unraveling the functional secrets of non-covalent molecular machines.
- To bridge the gap between static composition and dynamic cellular functions.
Main Methods:
- Review of recent literature on mass spectrometry (MS) applications.
- Focus on biophysical approaches.
- Analysis of MS techniques for studying non-covalent complexes.
Main Results:
- Recent MS developments offer powerful tools for structural biology.
- MS enables the study of dynamic interactions within molecular machines.
- Functional insights can be gained beyond mere protein identification.
Conclusions:
- Mass spectrometry is crucial for understanding the dynamic nature of molecular machines.
- Advanced MS techniques are essential for deciphering cellular regulatory mechanisms.
- This review emphasizes the pivotal role of MS in modern structural biology.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
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