Research in Dr. Thirumalai’s group focuses on various problems in equilibrium and non equilibrium statistical mechanics. Currently various aspects of the transition from liquid to amorphous state are being investigated. Another area of research involves the theoretical study of polymer-colloid interactions. Research is also being carried out to understand the dynamics of protein folding.
Major Recognitions and Honors
Over 30 students and postdoctoral fellows have trained with me. The majority of them are in academic positions.
Theoretical chemistry and Biophysics
The major focus of research in our group is to develop quantitative theoretical and computational methods to solve major problems in biology. We tackle a broad range of problems in biophysics using principles of statistical mechanics, polymer physics, and many computational techniques. Summaries of some of the areas that we are working on are given below.
Function of molecular chaperones: Although most proteins fold spontaneously in order to carry out their functions a few misfold, and can potentially aggregate. To guard against this aberrant phenomenon nature has evolved molecular chaperones that can recognize and rescue the misfolded structures. The most intensely studied chaperone is GroEL, which undergoes complex structural transformations in response to ATP binding. Together with Prof. George H. Lorimer we are working to provide a molecular basis for the function of this ATP-driven machine.
Single Molecule Force Spectroscopy: The ultimate dram of watching proteins and RNA fold one molecule at a time is starting to be realized with
advances in single molecule methods. In order to fully realize the scope these advances it is important to develop theoretical methods that can uncover the folding landscape of biomolecules using experimental input. We are developing some of the most advanced methods that provide mechanism of how proteins, RNA, and protein complexes respond to mechanical force.
Protein aggregation and link to diseases: It is now firmly established that a number of diseases (Alzheimer’s, Parkinson’s, mad cow disease etc) are linked to aggregation of specific proteins. The mechanisms of aggregation and their structures are largely unknown. We are using Molecular Dynamics
simulations to provide microscopic details of how low order aggregates form. The biophysical results provide clues in devising drugs that can prevent aggregation in proteins.