PhD Yale University, 2013
MS Indian Institute of Technology, Bombay, 2006
BS Jadavpur University, 2004
Physical and Biophysical Chemistry
Hydrophobic interactions play an important role in protein folding, and formation of lipid micelles and bilayers. Current opinion regarding the arrangement of water around small hydrophobic molecules is that it is akin to those found in clathrate hydrates of natural gases. My research group will utilize a broad range of techniques spanning the fields of physical and biophysical chemistry to better understand water dynamics in clathrates and biological systems.
Project 1: Studies on Clathrate Hydrate Systems
To gain a deeper understanding of the interaction between water and hydrophobic molecules, my group will use clathrate hydrates as a model system. Clathrate hydrates are solid inclusion compounds formed when guest molecules such as methane, ethane, propane, carbon dioxide, etc., occupy host water cages. While normal ice is composed of layers of puckered hexagonal rings of water molecules, clathrate structures are composed of different water cages. Although the H2O lattice of the hydrate is slightly less stable than that of hexagonal ice, the interaction with trapped gas molecules brings the free energy below that of the separated ice and gas. Using home-built equipment, students will be able to monitor the kinetics of clathrate hydrate formation from different gases and ice particles. The preliminary goal of this project is to characterize the change in hydrate formation kinetics, and host-guest dynamics in hydrate systems on addition of trace amounts of substances which perturb the host-guest interaction, such as alcohols and ionic solutes.
Project 2: Dynamics in water-regulation proteins
Aquaporins are a class of proteins that are involved in passive water transport across cell membranes in such varied tissues as liver cells, eye lens, intestines, etc. It should be noted that aquaporins transport water but prevent the transport of protons which are smaller and able to transfer through negatively charged sites. The goal of this project is to investigate the specific interactions between water and these proteins. The proteins will be expressed in bacterial or yeast cells with various isotopic labelling schemes suitable for solid-state NMR.