Protein Function and Dynamics

蛋白质功能和动力学

• 批准号: 8806113
• 负责人: Maurice Eftink
• 金额: $ 25.52万
• 依托单位: University of Mississippi
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-09-01 至 1992-02-29
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8806113&HistoricalAwards=false
• 关键词: Protein; Function; Dynamics

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.***//

该研究项目旨在a）进一步表征 所选蛋白质的内部动力学，B）关注 粘度、压力和温度对 蛋白质的动力学和功能; c）发展 荧光采集和分析协议， 物理模型之间真实准确的关系 和实验数据。 Eftink博士将使用 多频相位/调制荧光法和溶质 荧光猝灭反应来表征 在选择的氨基酸中单个色氨酸残基的发射 proteins. 蛋白质的动力学性质是一个问题， 对理解配体的重要性 结合，催化，协同效应，蛋白质-蛋白质 识别和其他功能方面的蛋白质。 是 显然，有一个重要的需要知道更多的比 蛋白质的静态三维结构， 揭开它们的功能之谜 分子动力 计算可以提供有洞察力的模拟， 事件，但这些计算必须始终得到指导和/或 由蛋白质的经验性实验测量支持 动力学 溶质猝灭和其他荧光技术 对目前的数据库做出了很大的贡献， 蛋白质在纳秒时间尺度上的波动。 这些荧光技术的进一步发展应 增强将生物物理动力学 模型与荧光数据。*//