Bio-Organic Biomedical Mass Spectrometry Resource
From BTRR
Overview
The resource focuses on mass spectrometric techniques for sequencing and quantitating peptides and structural characterization of modified proteins and glycoconjugates; microsample handling and mass spectrometric analysis at the femtomole to attomole level, such as in the identification of proteins separated by two-dimensional (2-D) gel electrophoresis using silver and fluorescence detection; cotranslational and posttranslational modifications of proteins, including glycosylation, phosphorylation, sulfation, and acylation; and xenobiotic modification, such as that arising from mechanism-based enzyme inhibition and drug-protein adduct formation. Methodology includes matrix-assisted laser desorption ionization with high-energy collision-induced dissociation analysis and capillary high-performance liquid chromatography (HPLC) nanoflow rate electrospray tandem mass spectrometry.
Current Research
Molecular and cellular proteomics, drug metabolic activation, and protein adduct identification; studies of protein machines, complexes and signaling cascades, and structural biology; studies of Conus peptides that are blockers of ion channels and neurotransmission. In addition, development of multidimensional ion exchange and reverse-phase separations of affinity-separated, isotopically labeled peptides from cell culture and in vivo systems using new acid-cleavable, carbon-13-coded ICAT reagents. Development of complementary offline chromatographic [matrix-assisted laser desorption ionization (MALDI-(CIDMS)] and online (ESI-CIDMS) strategies for comprehensive detection and sequencing of ICAT-labeled systems. Development of electrospray ionization and MALDI and tandem technologies for determination of biomolecular and structural studies of proteins, noncovalent and covalent protein assemblages, heterobiopolymers, and glycoconjugates.
