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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.
past nineteen 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 two graduate
students, a technician, and four undergraduate students. See a list or recent
publications by clicking below.
We have projects on the characterization of antibodies and other glycoproteins, 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 and are part of the MabNet Monoclonal Antiboby Network sponsored by NSERC.
TEACHING: Bioanalytical Chemistry
CHEM 2270, Elements of Biochemistry I: 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