We are motivated to develop analytical mass spectrometry methods for proteome profiling and protein structural characterization. Mass spectrometry is the pre-eminent technology in analytical biology. However, current practices on the front end of mass spectrometry analysis are not fully utilizing the potential of modern mass spectrometry technologies. The development of advanced analytical methods on the front end of mass spectrometry analysis is critical to advancing the study of biological sciences. The mass spectrometry-based methods we have developed include 1) proteolytic 18O labeling to measure the protein abundance in proteome samples, 2) histidine hydrogen-deuterium exchange mass spectrometry (His-HDX-MS) to probe protein structural changes, 3) isotope labeling method to determine the stoichiometry of lysine acetylation at individual sites, and 4) single-tube sample preparation method for shotgun proteomics. These methods have been effectively used to answer a range of biological questions.
Our current research interests include 1) developing an analytical method for identifying the targets of a drug, 2) developing a strategy for detecting iso-Asp formation in proteins, and 3) understanding the relationship of aggregatin post-translational modifications and its cellular localization.