Vibrational, Orientational, and Conformational Dynamics of Molecules in Solution

麻省理工学院的Andrei Tokmakoff教授得到了实验物理化学项目的支持，对蛋白质的超快动力学进行了实验研究。这项基础研究将探索控制蛋白质折叠的力的基础。PI将使用二维超快红外光谱和拉曼光谱来测量肽和蛋白质的酰胺带随温度、pH和溶剂的动态变化。该方法将以独特的方式探测振动耦合、能量耗散、溶剂-蛋白质相互作用和结构非均质性。蛋白质从大量可能的结构中获得预期的三维结构的过程尚不清楚，这是生物化学中尚未解决的主要问题。由于最近研究蛋白质折叠的计算方法取得了进展，因此提出的工作尤其及时。在这一领域的新实验是迫切需要的，PI提出了新的基于激光的方法，类似于核磁共振光谱中使用的方法。

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.