Welcome to Shashank Deep Biophysical Chemistry Lab

MS 729, Department of Chemistry, IIT Delhi, Hauzkhas, New Delhi

Congratulation to Preeti for acceptance of her paper in RSC Advances.

Congratulation to Nidhi K Bhatia for acceptance of her paper in BBA

Congratulation to Nidhi Katyal for acceptance of her paper in PCCP

Congratulation to Shivnetra for acceptance of her paper in JPC B.

Congratulation to Shahid for acceptance of his paper in Journal of Molecular Recognition.

Dr. Shahid M. Nayeem is now Associate Professor in Aligarh Muslim University.Congrats!

Ligand-receptor interaction: Ligand-receptor interactions are central to the most biological processes, and detection of specific amino-acid residues that contribute to the specificity and strength of protein interactions is a problem of the utmost importance. Within the vast interaction networks available for various biological processes, there is significant redundancy, with many proteins acting as "hubs" that recognize multiple binding partners, and yet also significant discrimination. The factors that bring a balance in favor of specificity and promiscuity in any protein-protein interactions are not clear and still under study. Understanding the balance is critical both from fundamental and applied perspectives. The clue to understand the complex biological phenomena lies at the molecular level described by physical terms and studied by physical methods. Structural information reveals one face of a receptor-ligand assembly, while the other face is revealed by the information on the energetic contribution of the interfacial residues to receptor-ligand assembly which is necessary for the design of inhibitors of minimum size and maximum affinity and specificity. Specificity in binding between receptor and ligands is being investigated using a combination of experimental, computational and molecular biology techniques.

Protein aggregation: The phenomenon of protein aggregation is important in widely different contexts such as food biochemistry, protein folding, neurodegenerative diseases, and preparation of protein pharmaceuticals. Despite the importance of the problem and nearly 50 years of research aimed at determining the mechanism for protein aggregation, many questions still remain unanswered. The complexities of the aggregation processes and the interwined events account for the fact that no effective disease modifying treatments for the aggregation related disorders are currently available. Rigourous combinations of the structural, kinetic and thermodynamic data are being used in our laboratory to get a great deal of insight into the process of aggregation.