THERMODYNAMICS OF LIGAND BINDING TO E COLI CHAPERONIN GROEL

GroEL分子伴侣蛋白与配体结合的热力学 E.使用等温滴定量热法探测大肠杆菌。 GroEL是一种帮助其他蛋白质折叠的热休克蛋白 无论是在体内还是体外。 在条件下， 未折叠底物蛋白不能自发折叠GroEL需要 K+、Mg2+、ATP水解和辅伴侣蛋白GroES。 的 每个配体结合的热力学将被单独检查 并与其它配体结合。 通过这些研究，我们希望 发现各配体对热力学的影响 的未折叠蛋白质，并将这些结果与激活 蛋白质折叠的能量。 这些研究将解决其中一个 伴侣蛋白折叠机制的主要未解决问题：如何 伴侣蛋白是否将未折叠蛋白结合的能量 和核苷酸诱导的构象变化 来提高折叠产量

The thermodynamics of ligand binding to the GroEL chaperonin protein from E. coli is probed using isothermal titration calorimetry. GroEL is a heat-shock protein that assists other proteins to fold correctly both in vivo and in vitro . Under conditions where an unfolded substrate protein cannot spontaneously fold GroEL requires K+, Mg2+, ATP hydrolysis, and a co-chaperonin protein, GroES. The thermodynamics of each ligand binding will be examined individually and in combination with other ligands. From these studies, we hope to discover the thermodynamic effect of each ligand on the thermodynamics of unfolded proteins, and compare these results to the activation energy for protein folding. These studies will address one of the major unresolved issues of chaperonin protein folding mechanism: How does the chaperonin transfer the energy of unfolded protein binding and a nucleotide-induced conformational change to enhance the folding yield?