Thermodynamics of Structural Fluctuations in Proteins

蛋白质结构波动的生物学作用 虽然他们的存在尚未建立， 充分证明。 这部分是由于不确定性， 这一现象的热力学基础。 可能性 范围从在限定的构象底物之间通过， 如在血红蛋白的变构模型中， 调节通道沿着的反应坐标， 酶底物复合物 罗森伯格博士将把计划中的研究建立在一个物理基础上。 他为这些现象建立的模型。 整体 目的是检验模型的有效性， 证明它在解释可能的 结构波动在生物过程中的作用。 他选择了良好的实验系统， 表征蛋白质并测试分析方法。 该项目的一个主要优势是多样性 方法学（氢交换，荧光猝灭， 热稳定性）应用于蛋白质的研究 动议

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.