Thermal proteome profiling: Insights into protein modifications, associations, and functions

Curr Opin Chem Biol. 2022 Dec:71:102225. doi: 10.1016/j.cbpa.2022.102225. Epub 2022 Nov 8.

Abstract

Tracking proteins' biophysical characteristics on a proteome-wide scale can provide valuable information on their functions and interactions. Thermal proteome profiling (TPP) is a multiplexed quantitative proteomics approach that measures changes in protein thermal stability-a key biophysical property-across different cellular states. Developed in 2014, as a target-deconvolution assay for drugs and other small molecules, TPP has since evolved to a system-level biochemical omics technique providing insights into context-dependent changes in protein states. In this review, we summarise key advances in the experimental and data analysis pipeline that have aided this transformation and discuss the recent developments and applications of TPP.

Keywords: Bottom-up proteomics; MS-CETSA; PTMs; Post-translational modifications; Protein complexes; Proteomics; TPP; Thermal proteome profiling.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Stability
  • Proteome* / metabolism
  • Proteomics* / methods

Substances

  • Proteome