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 twenty 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 spectrometer
in our laboratory is equipped with matrix-assisted laser desorption/ionization
(MALDI), and we also have HPLC systems for sample preparation. See a list of recent publications.
We have projects on the
characterization of antibodies and other glycoproteins, we work in
collaboration with medical researchers, microbiologists, biochemists and
government 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.
For pictures of our group click here.
TEACHING in 2016 (fall):
Analysis, CHEM 3590.
This is a half-year, 3 credit-hour fall
course. Visit the course web site for schedule and content (will be available
mid August 2016)