Overview

The Gomes group develops mass-spectrometry (MS)-based strategies to elucidate the structure of intact proteoforms and their complexoforms within cells. Our MS workflows benefit from chromatography, capillary electrophoresis, and ion mobility spectrometry. Bioinformatics, biochemical, and chemical biology tools are used to validate the biological relevance of our findings.  

Native Top-Down Characterization of Proteoforms and their Complexoforms

While native MS provides unparalleled information on the architecture, stoichiometry, and binding partners of intact protein complexes and their modified forms (complexoforms), top-down proteomics enables in-depth characterization of intact monomeric proteins and their modified forms (proteoforms). Recently, these two powerful MS strategies have been combined in a single MS strategy “native top-down proteomics (nTDP)” to provide detailed structural information about proteoforms and their complexoforms. We are currently developing nTDP strategies for the characterization of Nuclear Receptors and G protein-coupled Receptors within cells. 

Top-Down Analysis of Single Cells

Responses of subcellular populations are typically measured as an average of the signals of individual cells. But communication between individual cells can generate unique cell-to-cell information that cannot be obtained from the bulk analysis of cells due to the distinctive molecular compositions of each cell. Our group is currently developing top-down proteomics -based methods for the characterization of proteoforms in single cells.