Siddhartha P. Sarma
Much of our understanding of biomolecular structure, and by inference, their physico-chemical properties, have been made possible by X-ray crystallographic studies of such molecules. The behavior of molecules in the solution state is often significantly different from that in the solid state. NMR spectroscopy is the method of choice for the structure determination of biomolecules in solution at atomic resolution. The advent of multi-dimensional NMR methods has enabled the study of site-specific structural and physico-chemical properties of large, often complex molecules within a global context. Additionally, knowledge of structure has important implications for the design of new molecules that could function as pharmacological agents for therapeutic or diagnostic purposes. The research efforts in our laboratory focuses on, among others, structural properties of enzymes involved in metabolic pathways associated with amino acid, vitamin and nucleotide biosynthesis, disulfide rich peptide animal toxins, on intrinsically disordered proteins, aromatic interactions and their effects on protein stability. The structural and functional aspects of several enzymes and peptide toxins of animal origin are under investigation. A fusion protein system, based on the protein cytochrome b5 has been developed specifically for the production of isotopically enriched proteins for these NMR based investigations. In addition to NMR spectroscopy, the laboratory also uses Mass Spectrometry for characterization of natural peptide toxins.