Thermodynamics of Structural Fluctuations in Proteins

蛋白质结构波动的热力学

• 批准号: 8704740
• 负责人: Andreas Rosenberg
• 金额: $ 20万
• 依托单位: University of Minnesota-Twin Cities
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1987
• 资助国家: 美国
• 起止时间: 1987-09-01 至 1991-02-28
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8704740&HistoricalAwards=false
• 关键词: Thermodynamics; Structural; Fluctuations; Proteins

The biological role of structural fluctuations in proteins has not been established although their presence has been amply demonstrated. This is partly due to uncertainty about the thermodynamic basis for the phenomenon. Possibilities range from passage between defined conformational substrates, as in the allosteric model for hemoglobin, to pure kinetic regulation of the passage along the reaction coordinate of enzyme substrate complex. Dr. Rosenberg will base the planned research on a physical model that he has developed for these phenomena. The overall goal will be to test the validity of model and then demonstrate its usefulness in explaining the possible function of structural fluctuations in biological processes. He has selected sound experimental systems using well- characterized proteins and tested analytical methodologies. A major strength of this project is the diversity of methodologies (hydrogen-exchange, fluorescence-quenching, thermal stability) being applied to the study of protein motions.

蛋白质结构波动的生物学作用尚未确定，尽管它们的存在已得到充分证明。这部分是由于这种现象的热力学基础的不确定性。可能性的范围从在确定的构象底物之间传递，如血红蛋白的变构模型，到沿着酶底物复合物的反应坐标传递的纯动力学调节。罗森博格博士计划的研究将基于他为这些现象开发的物理模型。总体目标将是测试模型的有效性，然后证明其在解释生物过程中结构波动的可能功能方面的有用性。他选择了完善的实验系统，使用表征良好的蛋白质和经过测试的分析方法。这个项目的一个主要优势是方法的多样性（氢交换、荧光猝灭、热稳定性）被应用于蛋白质运动的研究。