College of Biological Sciences
Twin Cities
Functional characterization of the lysine acetylation pathway requires quantitative measurement of the modification abundance at the stoichiometry level. These researchers have developed a systematic workflow for global untargeted identification of site-specific Lys acetylation stoichiometries in mammalian cells. Their strategy includes an optimized protocol for in vitro chemical labeling of unmodified lysine with stable isotope-encoded acetyl-NHS ester, deep proteomic profiling with a high-resolution mass spectrometer, and a new software tool for quantitative analysis and stoichiometry determination.
The resources provided by MSI support the data analysis using the software tool for stoichiometry analysis and quantitative proteomics study. The group also uses MSI to develop new tools for data-mining tandem mass spectrometry spectra and identifying novel modification pathways.