Dataset Information

Integrated changes in thermal stability and proteome abundance during altered growth and metabolic cell states.Integrated changes in thermal stability and proteome abundance during altered growth and metabolic cell states.

ABSTRACT: Altered thermal solubility measurement techniques are emerging as powerful tools to assess ligand binding, post-translational modification, protein-protein interactions, and many other cellular processes that affect protein state under various cellular conditions. Thermal solubility or stability profiling techniques are enabled on a global proteomic scale by employing the latest generation of isobaric tagging reagents that facilitate multiplexing capacity required to measure the proteome across thermal gradients. Key among these is thermal proteomic profiling (TPP), which requires 8-10 isobaric tags per gradient and multiple sets of proteomic analyses to measure different replicates and conditions. Furthermore, using thermal profiling techniques to measure protein state across different conditions also requires measurements of difference in protein abundance. Here, we use PISA to assess protein abundance and thermal stability.

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ORGANISM(S): Escherichia Coli

SUBMITTER: J Patrick Murphy

LAB HEAD: J Patrick Murphy

PROVIDER: PXD031800 | Pride | 2024-02-14

REPOSITORIES: Pride

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Publications

Integrated changes in thermal stability and proteome abundance during altered nutrient states in Escherichia coli and human cells.

Sultonova Mukhayyo M Blackmore Beau B Du Ronnie R Philips Olivier O Paulo Joao A JA Murphy John Patrick JP

Proteomics 20220916 19-20

Altered thermal solubility measurement techniques are emerging as powerful tools to assess ligand binding, post-translational modification, protein-protein interactions, and many other cellular processes that affect protein state under various cellular conditions. Thermal solubility or stability profiling techniques are enabled on a global proteomic scale by employing isobaric tagging reagents that facilitate multiplexing capacity required to measure changes in the proteome across thermal gradie ...[more]

PMID: 36082775

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