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Proteins play very
important roles in all types of organisms. They can act as enzymes, catalysts,
oxygen carriers, structure building blocks, among many other possible roles.
Normal protein function results of a combination of amino acid sequence, 3-D
structure and sometimes aggregation with other proteins or biomolecules. If
sequence (thus often structure) is altered, protein function changes, possibly
causing diseases or other problems.
Over the past fifteen
years, we have been interested in characterizing modified proteins from several
sources, using mass spectrometry as our main analytical tool. Because proteins
in cells always occur in very complex mixtures, preliminary steps such as
electrophoresis and chromatography are often required in sample preparation.
The mass spectrometers in our laboratory are equipped with a range of
ionization methods, e.g. electrospray (ES) and matrix-assisted laser
desorption/ionization (MALDI). Our research group now counts four graduate
students, a technician and a research associate. See a list or recent
Fragmentation of a glycopeptide
At this stage, we have projects on the characterization of glycoproteins, phosphoproteins, modified enzymes. We work in collaboration with medical researchers, microbiologists, biochemists and industry researchers. We also analyze samples as a service to our Department and to the scientific community.
Sequencing a peptide by tandem mass spectrometry
TEACHING: Bioanalytical Chemistry
CHEM 1000, Understanding the World through Chemistry: This is a half-year, 3 credit-hour fall course. Visit the course web site for schedule and content.
CHEM 4590, Advances Bioanalytical Chemistry: This is a half-year, 3 credit-hour winter-spring course. Visit the course web site for a tentative course schedule.
RESEARCH PUBLICATIONS: click here
Last updated July 19, 2013