Structural biology, X-ray crystallography, biophysical characterization of the signaling components of the visual signal transduction pathway, protein-ligand interactions using SH3-domain containing proteins, blue-light photoreceptors of the LOV family, natively unfolded proteins, protein aggregation using dynamic light scattering and CD spectroscopy.
The primary focus of our research is to understand the structure-function relationships of soluble and membrane proteins of biological importance. Our approach remains to conduct these studies with techniques that allow a complete dissection of kinetic and structural properties of the proteins in static and dynamic states. The functional and thermodynamic properties on wild-type and modified forms of the macromolecules generated by site-directed mutagenesis are studied extensively using transient and steady-state kinetics, as well as selected biophysical techniques. The functional information is then combined with the three-dimensional structure determined by X-ray crystallographic techniques.