Protein-folding and protein solvent interactions: Understanding protein folding interamediates qualitatively and quantitatively is an essantial step in unraveling the protein folding code. Further, the stability of a protein under specific conditions depends on its interactions with the solvent environment. Our group focuses on understanding protien folding intermediates, protein-solvent interactions, and protein stabilization by using a combination of calorimetric, spectroscopic, and molecular simulation methods. 

Drug-protein interactions: We are interested in understanding physical chemistry underlying drug-protein interactions in the absence and presence of drug delivery systems. The work is focused on understanding the guidelines for the target-oriented drug-delivery. Here, also a combination of calorimetric and spectroscopic techniques are being employed.

Prevention of aggregation/fibrillation in proteins: We are interested in understanding the nature and energetics of interactions between potential inhibitors and proteins which leads to inhibition process. 

Building block-solvent interactions: We attempt to study fine details of interactions of biologically important molecules with solvent environment by measuring physiochemical properties of the buliding blocks in chosen solvent environment.