Research Interests

Polypeptides (proteins) and polynucleotides (DNA, RNA) are the most prevalent biological macromolecules. While DNA is responsible for data storage and transmission, proteins are the functional blocks that make a viable living organism. The function of a protein is directly correlated with the spatial disposition of its atoms. Macromolecular crystallography is a powerful method for obtaining the three dimensional atomic structure of large biological molecules, that provides a wealth of information that are being used in many aspects of research, including structure-based drug design. Elucidation of the structures of lysozyme and proteases were the first to show exactly how proteins bind their substrates and enzymatically catalyze chemical reactions. The structures of hemoglobin in both oxy- and deoxy- forms showed that proteins alter their spatial arrangement to modulate their function. Thus having the 3D structure of a protein has immense benefits.

Our group works on the structural and functional characterization of novel proteins from pathogenic organisms. We characterize these proteins in comparison with human homologues and differences therein are utilized for the development of novel inhibitors against pathogens. The study includes aspects of molecular biology, protein biochemistry, computationa biology and bioinformatic analysis, X-ray crystallography, Small Angle X-ray scattering. The proteins being explored in our lab include membrane transporters like ion transporters, ABC transporters, transferases, structural proteins and metabolic proteins from the polyamine biosynthesis pathway, purine salvage pathway of Leishmania and proteins involved in transcription machinery of Vibrio cholerae.
The group is also interested in the mechanistic aspects of helical assembly, especially in coiled-coils and helical bundles.