TIME RESOLVED SAXS STUDIES OF PROTEIN FOLDING

使用时间分辨小角X射线散射(SAXS)，我们将 测量未折叠蛋白质所经历的压缩速度 它突然被置于原生条件下。SAXS是唯一的 时间分辨实验探测器，可以给出总尺寸和 蛋白质构象状态的形状指示。SAXS数据 可用于确定回转半径；以获得形状 可以从Kratky情节和这对情侣中推断的信息 分布函数；并确定 蛋白质样本。细胞色素c的时间分辨SAXS测量 重新折叠显示了死者体内联想状态的形成 停流混合器的时间。我们已经证明， 可以通过使用较低的蛋白质浓度和 较高的最终变性剂浓度。

Using time-resolved small-angle x-ray scattering (SAXS), we will measure the rate of compaction undergone by an unfolded protein when it is suddenly placed under native conditions. SAXS is the only time-resolved experimental probe which can give an overall size and shape indication of the conformational state of a protein. SAXS data may be used to determine the radius of gyration; to obtain shape information which may be inferred from the Kratky plot and the pair distribution function; and to determine the association state of a protein sample. Time-resolved SAXS measurements of cytochrome c refolding show the formation of an association state within the dead time of the stopped-flow mixer. We have shown that the degree of association can be reduced by using lower protein concentration and a higher final denaturant concentration.