Much of the research activity is focused toward the development and application of mass spectrometry for the analysis of intact peptides, proteins, protein–protein, and protein–RNA/DNA complexes. Recent studies have included: identification of platination sites in peptides (bombesin, substance P, angiotensin, bradykinin) using Infrared multiphoton dissociation (IRMPD), Collision-induced dissociation (CID) and Electron-capture dissociation (ECD), accurate mass measurements on intact proteins (YdaE 6.5kDa, ubiquitin 8.6kDa, trypsinogen 24kDa, carbonic anhydrase 28kDa, beSOD 31kDa, FbpA 33kDa, BSA 66kDa) under native and denaturing conditions, identification of dynamic post-translational modifications in intact human histones using top-down ECD, top-down identification of proteins from complex mixtures, as well as accurate mass analysis of oligonucleotide DNA strands (40 bp).
