Protein Function and Dynamics

该研究项目旨在a)进一步表征选定蛋白质的内部动力学，b)重点研究粘度、压力和温度对蛋白质动力学和功能的影响，以及c)开发荧光采集和分析方案，以便在物理模型和实验数据之间建立更真实和准确的关系。Eftink博士将使用多频相位/调制荧光法和溶质荧光猝灭反应的方法来表征选定蛋白质中单个色氨酸残留物的发射。蛋白质的动力学性质对于理解蛋白质的配体结合、催化、协同效应、蛋白质-蛋白质识别和其他功能方面具有重要意义。显然，为了揭开蛋白质功能的奥秘，我们需要知道的不仅仅是蛋白质的静态三维结构。分子动力学计算可以提供对可能事件的有洞察力的模拟，但这些计算必须始终以蛋白质动力学的经验实验测量为指导和/或支持。溶质猝灭和其他荧光技术对目前关于蛋白质在纳秒时间尺度上的波动的数据库做出了很大贡献。这些荧光技术的进一步发展将增强将光物理动力学模型与荧光数据联系起来的能力。

This research project is designed to a) further characterize the internal dynamics of selected proteins, b) focus on the effects of viscosity, pressure and temperature on the dynamics and function of proteins and c) develop fluorescence acquisition and analysis protocols for a more realistic and accurate relationship between physical models and experimental data. Dr. Eftink will use the methods of multi-frequency phase/modulation fluorometry and solute fluorescence quenching reactions to characterize the emission of individual tryptophan residues in selected proteins. The dynamic properties of proteins are a matter of fundamental importance in the understanding of ligand binding, catalysis, cooperative effects, protein-protein recognition and other functional aspects of proteins. It is clear that there is an important need to know more than the static three-dimensional structure of proteins in order to unravel the mysteries of their function. Molecular-dynamics calculations can provide insightful simulations of possible events, but these calculations must always be guided and/or supported by empirical experimental measures of protein dynamics. Solute quenching and other fluorescence techniques have contributed greatly to the present data base regarding the fluctuations in proteins on the nanosecond time scale. Further development of these fluorescence techniques should enhance the ability to relate photophysical kinetic models to fluorescence data.***//