Thermal proteome profiling: Insights into protein modifications, associations, and functions
Cecile Le Sueur1, Henrik M Hammarén2, Sindhuja Sridharan3
1European Molecular Biology Laboratory, Genome Biology Unit, 69117 Heidelberg, Germany; Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Current Opinion in Chemical Biology
|November 11, 2022
Summary
Thermal proteome profiling (TPP) measures protein thermal stability to reveal cellular states. This review covers TPP
Area of Science:
- Proteomics
- Biophysics
- Systems Biology
Background:
- Protein biophysical characteristics offer insights into function and interactions.
- Thermal proteome profiling (TPP) quantifies protein thermal stability across cellular states.
- Initially a drug discovery assay, TPP has evolved into a systems-level omics technique.
Purpose of the Study:
- To review advances in the experimental and data analysis pipeline of TPP.
- To discuss recent developments and applications of TPP.
Main Methods:
- Multiplexed quantitative proteomics.
- Measurement of protein thermal stability.
- Analysis of proteome-wide thermal stability changes.
Main Results:
- TPP has transformed from a target-deconvolution assay to a systems-level technique.
- Key advances in experimental and data analysis have driven TPP's evolution.
- TPP provides insights into context-dependent protein state changes.
Conclusions:
- TPP is a powerful tool for understanding protein behavior in different cellular contexts.
- Continued advancements enhance TPP's utility in biological research.
- TPP applications span various fields, offering a systems-level view of proteomes.
Keywords:
Bottom-up proteomicsMS-CETSAPTMsPost-translational modificationsProtein complexesProteomicsTPPThermal proteome profilingMore Related Videos
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