Vibrational, Orientational, and Conformational Dynamics of Molecules in Solution

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Professor Andrei Tokmakoff of MIT is supported by the Experimental Physical Chemistry program to perform experimental studies on the ultrafast dynamics of proteins. This fundamental study will probe the basis for the forces that govern protein folding. The PI will use two-dimensional ultrafast infrared spectroscopy and Raman spectroscopy to measure the dynamics of the amide bands of peptides and proteins as functions of temperature, pH and solvent. The method will probe vibrational couplings, energy dissipation, solvent-protein interactions and structural heterogeneity in a unique way. The process by which proteins attain their intended 3 dimensional structures from a very large number of possible structures is not well understood, and this is a major unsolved problem in biochemistry. The proposed work is especially timely because of recent progress in computational methods for studying protein folding. New experiments in this area are critically needed and the PI proposes novel laser based approaches in analogy to methods utilized in Nuclear Magnetic Resonance spectroscopy.