KLEIN PRT TIME (LBNL)

了解金属蛋白质相互作用的核心是 一直是关于金属是否会强制执行特定的第四季的问题 蛋白质的结构或蛋白质是否传递特定的 金属上的协调环境。几个两亲性的，a-螺旋的 多肽已经被重新设计以允许直接的 金属蛋白定义因素的实验测定 互动。通过将半胱氨酸残基放入 捆绑生成金属结合部位，我们可以直接测试 特定束的稳定性和金属离子的作用 配位几何改变了这种稳定性。我们选择了一个 一系列具有配位偏好的亲硫型金属 包括2个坐标(线性)、3个坐标(三角)和4个 配位(四面体)推论热力学稳定性 与这些不同环境中的金属结合有关。这个 要研究的金属是锌(II)、汞(II)、镉(II)、铜(I)、银(I)和 文书主任(II)除作为对照的Co(II)外， 除了EXAFS之外，没有其他技术可以提供明确的 局部金属位置结构的表征。

Central to the understanding of metal protein interactions has been the question of whether metals enforce specific quarternary structure in proteins or whether proteins impart a specific coordination environment on the metal. Several amphiphilic, a-helical peptides have been designed de novo in order to permit a direct experimental determination of the factors which define metal protein interactions. By placing cysteine residues into the interior of the bundle to generate metal binding sites, we can test directly the stability of a particular bundle and the role of metal-ion coordination geometry in altering this stability. We have chosen a series of thiophilic metals that have coordination preferences including 2 coordinate (linear), 3 coordinate (trigonal) and 4 coordinate (tetrahedral) to deduce the thermodynamic stabilities associated with metal binding in these different environments. The metals to be studied are Zn(II), Hg(II), Cd(II), Cu(I), Ag(I) and Co(II). With the exception of the Co(II), which serves as a control, there is no technique other than EXAFS that can provide unambigous characterization of the local metal-site structure.