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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: Jul 2, 2025

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

Experimental and data analysis advances in thermal proteome profiling.

Amanda M Figueroa-Navedo¹, Alexander R Ivanov¹

¹Barnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA.

Cell Reports Methods

|February 27, 2024

Summary

This summary is machine-generated.

This review details advancements in mass spectrometry (MS)-based thermal shift assays for studying drug-protein interactions. It highlights method development and data analysis improvements for enhanced sensitivity and accuracy in proteomic profiling.

Keywords:

CP: biotechnology cellular thermal shift assays drug discovery protein-ligand interactions target engagement thermal proteomic profiling

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Last Updated: Jul 2, 2025

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

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Published on: June 8, 2020

Area of Science:

Biochemistry
Proteomics
Pharmacology

Background:

Mass spectrometry (MS)-based thermal shift assays are crucial for characterizing drug-protein interactions.
Understanding protein-ligand interactions is vital for drug discovery and development.
Current methods require thorough investigation for improved sensitivity and accuracy.

Purpose of the Study:

To review method development in MS-based thermal shift proteomic assays.
To identify areas for improvement in data analysis for thermal proteome profiling.
To optimize experimental strategies for more reliable protein-ligand interaction studies.

Main Methods:

Discussion of data processing for MS-based thermal proteome profiling.
Evaluation of method development's impact on assay sensitivity and accuracy.
Overview of experimental strategy optimization, emphasizing biological replicates.

Main Results:

Method development significantly impacts the sensitivity and accuracy of thermal proteome profiling.
Improvements in data processing and analysis enhance the quality of thermal proteome profiles.
Prioritizing biological replicates over evaluated temperatures improves experimental robustness.

Conclusions:

Optimized method development and data analysis are essential for reliable MS-based thermal shift assays.
Enhanced experimental strategies, including sufficient biological replicates, are key to advancing drug-protein interaction studies.
This review provides a framework for improving thermal proteome profiling in drug discovery.