2.            Structure and function studies on M. tuberculosis heat shock proteins

                We have been interested in the overall properties of the M. tuberculosis HSPs, not that these are likely to be different than those of other well-studied prokaryotes.  However, recent literature suggests that the HSPs play an important role in the pathogenesis of M. tuberculosis, and therefore our interest in this family of proteins.  Our focus till now has been on the Hsp10 (GroES or Cpn10) and the two Hsp60’s (GroEL-1/ GroEL-2 or Cpn60.1/ Cpn60.2).  We have also initiated studies towards biophysical and structural characterization of the two major heat shock repressors: HspR and HrcA.

3.            Structure and function studies on redox enzymes of M. tuberculosis

                Redox processes play an important role in the physiology of M. tuberculosis. Since, M. tuberculosis spend substantial amount of time in the phagosomal milieu of host macrophages, it is believed that modulation of the redox reactions might help M. tuberculosis survive the hostile environment therein. We are interested in the structure and biochemical characterization of redox reactions in M.tuberculosis, with the hope that this will offer useful insights into the natural resistance of Mycobacteria towards oxidative killing. Towards achieving this objective, we have undertaken analysis of M. tuberculosis thioredoxins, alkylhydroperoxidase and inositol-1-phosphate synthase.

4.            Large scale analysis of protein:protein interactions networks

                Cellular functions are determined by intricate interactions among many components of cells.  Proteins being the dominant molecules of life, interactions among all the cellular proteins direct many of the cellular responses.  We have recently become interested in the analysis of genome-wide protein:protein interactions.  Our interest primarily is in applying graph theory to protein:protein interactions and attempt to understand how cells respond to external environmental signals.

5.            Obtaining insights into biochemical functions of proteins using 3D structural knowledge

                One of the paradigms that has evolved in modern biology states that the functional properties are conferred on proteins by virtue of their overall shape and conformation. In the post-genomics era, when sequences are becoming rapidly available, the gap between the availability of sequences and understanding their functions is ever-widening. It is in this context we are attempting to analyse structures of proteins so that they can be assigned biochemical functions based on their 3D conformation.