ANOMALOUS X-RAY-SCATTERING FROM TERBIUM-LABELED PARVALBUMIN IN SOLUTION
ANOMALOUS X-RAY-SCATTERING FROM TERBIUM-LABELED PARVALBUMIN IN SOLUTION
复制标题
DOI：
10.1016/s0006-3495(83)84440-3
复制
发表时间：
1983-01-01
影响因子：
3.4
通讯作者：
HODGSON, KO
中科院分区：
文献类型：
--
作者：
MIAKELYE, RC;DONIACH, S;HODGSON, KO
用异常小角x射线散射作为结构探针，对Tb标记兔小白蛋白溶液进行了检测。这种技术利用了当x射线能量在这个重原子标签的L3吸收边缘附近调谐时，Tb散射因子发生的巨大变化。这些散射的变化导致标记蛋白的整体小角散射曲线的变化，然后可以对其进行分析，从而获得有关标记在蛋白质中分布的结构信息。根据蛋白质电子密度的高斯模型，从Tb到蛋白质质心的平均距离为13.2 . ang。并且与晶体学结果一致。这些结果证明了Tb作为异常散射标签的有效性，并提供了帮助将异常散射作为溶液中蛋白质的可靠结构技术的标准。
Anomalous small-angle X-ray scattering was used as a structural probe for solutions of rabbit parvalbumin labeled with Tb. This technique makes use of the large changes in the Tb scattering factor that occur when the X-ray energy is tuned around an L3 absorption edge of this heavy-atom label. These changes in scattering result in changes in the small-angle scattering curve of the labeled protein as a whole, when can then be analyzed to derive structural information concerning the distribution of labels in the protein. Based on a Gaussian model for the protein electron density, the mean distance from the Tb to the protein center of mass is 13.2 .ANG. and is consistent with crystallographic results. These results demonstrate the usefulness of Tb as an anomalous scattering label and provide criteria to help establish anomalous scattering as a reliable structural technique for proteins in solution.