Our research focuses on the use of mass spectrometry to answer biological questions. The majority of our projects involve characterizing the post-translational modifications (e.g., glycosylation, phosphorylation) present in the protein of interest. For example, we are currently investigating the in vivo changes that occur in human eye lenses upon normal aging and cataract formation. We hope that this research ultimately will provide a mechanism to prevent cataracts. Other projects involve the analysis of lipids and oligonuleotides. We rely on a variety of chromatographic and mass spectrometric (MS) techniques to perform these analyses, including capillary electrophoresis, high-pressure liquid chromatography, fast atom bombardment-MS, electrospray ionization-MS, high-performance liquid chromatography/MS, matrix-assisted laser desorption MS, and tandem MS. We also conduct research into developing new methodologies to increase the amount of information obtained from these MS experiments and to reduce the quantity of material needed for analysis
M.J. Kieliszewski, M. O'Neill, J. Leykam and R. Orlando, "Structure Determination by Tandem Mass Spectrometry of Glycopeptides in a Pronase Digest of the Proline-hydroxyproline-rich Glycoprotein from Douglas Fir", J. Biol. Chem. 1995, 270, 2541.
S. He, S. Pan, K. Wu, I.J. Amster and R. Orlando, "Analysis of Normal Human Fetal Eye Lens Crystallins by High Performance Liquid Chromatography/Mass Spectrometry", J. Mass Spectrom. 1995, 30, 424.