Binding Energetics and Dynamic Processes in Protein Dimers

生物特异性的本质在于能量学， 蛋白质-配体复合物的动力学和结构方面。 尽管人们一直在强调 蛋白质结构方面的阐明，主要是 通过使用X射线衍射研究， 配体结合和酶催化不能在 缺乏对宇宙的能量学和动力学的知识， 系统. 在过去的十年中，各种技术，如核磁共振， 氢交换和荧光光谱已经证明 蛋白质是动态分子 理论治疗，如 因为分子动力学计算也预测了 蛋白质残留物 这张蛋白质分子的照片 它与僵硬的、静态的 早期的X射线衍射研究所建议的描述。 目前正在集中精力阐明 这些运动对酶催化的功能意义， 配体结合的能量学 詹姆森博士将检查配体结合和亚基-亚基 苹果酸脱氢酶，细胞质苹果酸 脱氢酶和延伸因子荧光法 光谱学、高静水压和酶动力学 测量. 荧光光谱允许 确定作为环境函数的寿命， 蛋白质中的自旋动力学。 高压 技术目前正越来越频繁地被应用 生物分子的研究，因为内在的 与其他技术相比， 温度变化。

The essence of biological specificity resides in the energetics, dynamics and structural aspects of protein-ligand complexes. Although a great deal of emphasis has been placed upon elucidation of the structural aspects of proteins, primarily through the use of X-ray diffraction studies, the understanding of ligand binding and enzyme catalysis cannot proceed in the absence of knowledge of the energetics and dynamics of the systems. During the past decade diverse techniques such as NMR, hydrogen exchange and fluorescence spectroscopy have demonstrated that proteins are dynamic molecules. Theoretical treatments such as molecular dynamics calculations have also predicted motions of protein residues. A picture of the protein molecule has thus developed which is quite different from the rigid, static descriptions suggested by earlier X-ray diffraction studies. Considerable effort is now being focused on elucidating the functional significance of these motions to enzyme catalysis and the energetics of ligand binding. Dr. Jameson will examine ligand binding and subunit-subunit interactions in malate dehydrogenase, cytoplasmic malate dehydrogenase and elongation factor using fluorescence spectroscopy, elevated hydrostatic pressure and enzyme kinetic measurements. Fluorescence spectroscopy permits the determination of lifetimes as a function of environment and rotation dynamics of tryptophans in proteins. High pressure techniques are currently being applied with increasing frequency to the study of biological molecules because of the intrinsic advantages of the technique as compared to other techniques such as temperature variation.