Protein Crystals
PB group members
Crystal mounting
Diffraction image
Protein Purification
Crystallization drop set up
X-ray diffractometer
Crystal freezing
Protein structure and electron density
Diffraction data collection
Department of Biosciences and Bioengineering
Indian Institute of Technology Bombay
Proteins are important biological macromolecules as they play key roles in almost every biological process of a living organism. Protein molecules function as enzymes, transporters, mechanical strength enhancers, protective immune systems, signal transducers, etc. Three dimensional structure of a protein dictates its functional properties. Hence, determination and understanding of three dimensional structure a protein is essential for deciphering the mechanistic details about how a protein performs its activities. Our research group at IIT Bombay is focused in elucidating the structure-function relationship of proteins, rational design of enzymes and structure based drug development. We determine crystal structures of proteins. We perform extensive biochemical and biophysical studies on proteins, which enables us to obtain information complementary to that obtained from structure analysis. Recently we have determined several crystal structures of proteins including a very high resolution (1.25 Å) crystal structure of a sugar binding protein complexed with glucose. The crystal structures on P. falciparum plasmepsins (PMs) complexed with KNI compounds solved in our group provide detailed molecular insights for antimalarial drug development. We also perform molecular dynamics simulations in order to capture different dynamic motions and interactions in proteins and their complexes.
We have performed extensive structural studies on glutamate dehydrogenase (GDH) to decipher the catalytic mechanism and for understanding the molecular basis of cofactor recognition of this enzyme. Following movie presents some of the exciting structural features of Aspergillus niger GDH (AnGDH) complexed with substrate alpha-ketoglutarate (AKG) and cofactor NADP.
Our structural and biophysical studies indicate a novel mechanism of activation of vacuolar plasmepsins. Following videos show the structural changes during the activation of histo-aspartic protease (HAP), a vacuolar PM.
