Our research interests are primarily focused on the investigation of the three-dimensional structures and properties of biological molecules, particularly proteins and nucleic acids, in atomic detail and their correlation with biological activity. The methods we use are largely multidimensional and multinuclear NMR techniques. Besides, we use variety of methods based on optical spectroscopy, including fluorescence and circular dichroism. Recently, we started using isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) and Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF; TofSpec 2E) in our experimental studies. Besides we also use the techniques of protein chemistry and molecular biology for biosynthetic expression of proteins and their site-directed mutagenesis.

We have close links with the European Union Large Scale Facility for Nuclear Magnetic Resonance in life sciences (CERM) at Florence, Italy. This was first as part of the Department of Science and Technology (DST) sponsored Indo-Italian collaborative research project entitled "Structure and dynamics of calcium binding proteins". Presently, we have Marie Curie International Research Staff Exchange Scheme [Call identifier: FP7-PEOPLE-2009-IRSES (WW-NMR)] under the Seventh Framework Programme of European Union.