A look through our publications will reveal that we have a large diversity of interests.

We are excited by many different aspects of protein science, design and engineering, including the study of sequence-structure, structure-stability, structure-function, and structure-interaction relationships in proteins. We are also interested in some aspects of protein misfolding and malfunction through aggregation, degradation and mutations. In addition, we are interested in protein condensation through phase separation, under conditions of molecular crowding. 

The approach of our lab is best described as follows:

If we find something interesting, exciting, or useful about any protein, and have the bandwidth available to explore it, we will certainly move to deploy a certain fraction of our time, attention, and resources to do so, if nobody objects and if there are researchers willing to explore it, in the lab. Sometimes our motive would be to derive pleasure from understanding how nature deploys different designer proteins to different tasks. Sometimes our motive would be to derive satisfaction from applying that understanding to a real-life problem. 

We believe that the principles underlying natures design of proteins and their folding, stability and function have not yet been worked out.Therefore, we must study as many proteins systems as we can, and study different proteins in as many ways as we can, to move towards deciphering those mysterious principles that encapsulate the central dogma of molecular biology, at the terminal end of which proteins produced through gene expression must assuredly fold and function in predetermined ways. It is a life-long quest to figure out how nature does this, using all available scientific tools.