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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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Updated: Jun 18, 2025

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

Toward the analysis of functional proteoforms using mass spectrometry-based stability proteomics.

Ji Kang¹, Meena Seshadri¹, Kellye A Cupp-Sutton¹

¹Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK, United States.

Frontiers in Analytical Science

|July 29, 2024

Summary

Stability proteomics methods like TPP, SPROX, and LiP reveal protein structure changes from post-translational modifications (PTMs). Integrating these with top-down mass spectrometry will advance proteoform stability analysis.

Keywords:

mass spec protein thermal stability proteoform proteomics top-down proteomics

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Area of Science:

Proteomics
Biochemistry
Molecular Biology

Background:

Functional proteomics investigates protein functions, pathways, and mechanisms in cellular systems and diseases.
Stability proteomics measures protein resistance to denaturation or proteolysis to assess functionality.
Methods assess thermal stability of thousands of proteins in complex biological samples.

Purpose of the Study:

To review the application of stability proteomics methods for observing post-translational modification (PTM)-induced structural changes.
To explore the characterization of protein structural changes caused by PTMs and mutations.
To discuss future integration of mass spectrometry with stability proteomics for intact proteoform analysis.

Main Methods:

Thermal proteome profiling (TPP)
Stability of proteomics from rates of oxidation (SPROX)
Limited proteolysis (LiP)

Main Results:

Stability proteomics methods effectively observe PTM-induced structural changes impacting protein stability.
These techniques are valuable for drug target identification by observing stability shifts upon ligand binding.
Recent applications include characterizing structural effects of PTMs and mutations on protein function.

Conclusions:

Stability proteomics offers insights into PTM-induced structural dynamics and protein function.
Integrating top-down mass spectrometry with stability proteomics will enable intact proteoform stability characterization.
This integration promises a deeper understanding of the functional implications of variable protein modifications.