Our laboratory has a long-standing interest in the relationship between macromolecular structure and function, in particular the role of cat ions and anions in modulating protein conformation and enzyme activity. Currently most of our effort is focused in two areas: (1) the factors modulating the ryanodine receptor and (2) the interaction between capsular polysaccharide and two proteins, immunoglobin and complement factor C3.
The ryanodine receptor is an intracellular calcium channel best characterized in muscle cells where it forms a critical element of the excitation-contraction coupling process. Recent studies suggest that the ryanodine receptor may also be responsible for modulating calcium ion levels in other cell types.
Virulence of many pathogens is associated with the production of a polysaccharide capsule surrounding the organism. We are investigating the nature of the protein-polysaccharide interaction to understand the disease process itself as well as to gain new insights into carbohydrate-mediated events in intra- and intercellular communication.
We use a variety of physical techniques in our research including analytical ultra centrifugation, computational biochemistry, molecular visualization, spectrofluorimetry and other forms of optical spectroscopy, kinetic and thermodynamic analysis
