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Structure-function correlations in proteins, peptide hormones and drags

In biology, as elsewhere, form and function are intricately related.  In our laboratory, we try to relate the structures of biomolecules with their functions.

Antifreeze Proteins (AFPs)

Several cold-water fish make AFPs to
lower their serum freezing point and  hereby avoid death. Using physical methods, we have obtained the structure of several AFPs.  We have also made some synthetic AFPs. Collaborating with other Canadian scientists, we hope to solve the mystery of AFP action.

Collagen-Related Enzymes.

Using synthetic peptide substrates,
we have mapped the active sites of the enzymes that hydroxylate proline and lysine in collagen, the most abundant body protein. A similar approach is being pursued on collagenase whose action is important in arthritis, tumour and wound healing. We overexpress
collagenase  domains  and  determine  their  structures  by spectroscopic methods and by site-directed  mutagenesis.

Hormones and Drugs.

Design of potent hormone/drug depends
on knowing its receptor-bound conformation. We had hypothesized this to be the Ca²⁺ bound form of the hormone/drug. Using CD, fluorescence, NMR and modeling computations, we study the structures of peptide hormones and calcium channel drugs and their interactions with Ca²⁺and lipid membrane. We are trying to overexpress transmembrane segments of selected receptors and ion channels to assess the role of Ca²⁺ in signal transduction.