Vibrational, Orientational, and Conformational Dynamics of Molecules in Solution

溶液中分子的振动、取向和构象动力学

• 批准号: 0079268
• 负责人: Andrei Tokmakoff
• 金额: --
• 依托单位: Massachusetts Institute of Technology
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-08-01 至 2003-07-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=0079268&HistoricalAwards=false
• 关键词: Vibrational; Orientational; Conformational; Dynamics; Molecules

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.

麻省理工学院的Andrei Tokmakoff教授得到了实验物理化学计划的支持，对蛋白质的超快动力学进行实验研究。 这项基础研究将探索支配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酰胺谱带随温度、pH值和溶剂变化的动力学。 该方法将探测振动耦合，能量耗散，溶剂-蛋白质相互作用和结构异质性以独特的方式。蛋白质从大量可能的结构中获得其预期三维结构的过程尚未得到很好的理解，这是生物化学中未解决的主要问题。 由于最近在研究蛋白质折叠的计算方法方面取得了进展，因此建议的工作特别及时。 在这一领域的新实验是迫切需要的，PI提出了新的激光为基础的方法，类似于核磁共振光谱法中使用的方法。