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。 虽然 大量的重点放在阐明 蛋白质的结构方面，主要是通过使用X射线 衍射研究，对配体结合和酶的理解 如果没有能量学的知识，催化就不能进行。 和系统的动态。 在过去的十年里， 例如NMR、氢交换和荧光光谱， 证明了蛋白质是动态分子。 理论 分子动力学计算等方法也预测了 一些蛋白质残基的运动。 一张蛋白质分子的图片 因此，它与刚性的，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功能性 这些运动的意义，酶催化和能量学 配体结合 詹姆森博士将检查配体结合和亚基-亚基相互作用 在苹果酸脱氢酶、细胞质苹果酸脱氢酶和伸长中 因子使用荧光光谱法，提高静水压力 和酶动力学测量。 荧光光谱允许 确定作为环境和旋转函数的寿命 蛋白质中的双氢动力学。 高压技术是 越来越多地应用于生物分子， 与温度效应相比，该技术的优势。

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 some proteins 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 becoming more applied to biological molecules because of the intrinsic advantages of the technique compared to temperature effects.