Our research interest is focused on structure-function studies of proteins using high-resolution solution NMR, circular dichroism (CD) and fluorescence spectroscopy techniques.
Three-dimensional structures of proteins dictate the specificity and diversity of their biological functions. The key to understanding the molecular mechanisms of their functions is to determine the underlying structural elements that are responsible for a specific functional activity. To achieve this goal, we are keenly interested in the determination and characterization of the high-resolution atomic structures of proteins, protein-ligand and protein-protein complexes to understand the mechanisms of their functions and mode of interactions using primarily NMR and other biophysical techniques. The following three different model systems are under study in our laboratory.
Biochemistry, Structural Biology, Molecular Biology, and Computational Chemistry: Cloning, expression, purification and 3-dimensional structure determination of proteins by NMR and X-ray crystallography, mutagenesis and functional studies of proteins involved in cancer, various signaling pathways and many diseases.
