CROSS-BETA CONFORMATION IN PROTEINS
CROSS-BETA CONFORMATION IN PROTEINS
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DOI：
10.1016/0022-2836(68)90014-4
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发表时间：
1968-01-01
影响因子：
5.6
通讯作者：
BEIGHTON, E
中科院分区：
文献类型：
--
作者：
GEDDES, AJ;PARKER, KD;BEIGHTON, E
提出了一种结构来解释自然发生的交叉纤维蛋白的x射线衍射图样。定向良好的纤维含有约25[度]A厚的带状胶束，其最长尺寸平行于纤维轴。带面对面包装，界面间距平均为15[正负]4 a。条带的内部结构基本上与Marsh， Corey & Pauling（1955）所描述的柞蚕丝模型相同，但在交叉P构象中，多肽链的延伸部分与纤维轴成直角。在所研究的蛋白质中，这些延伸的部分通过短的“弯曲”区域连接在一起，形成连续的折叠多肽链，这些多肽链位于与带状胶束表面垂直的平面上，并平行于它们的长轴。
A structure is proposed to explain the X-ray diffraction pattern of a naturally occurring cross- [beta] fibrous protein. The well-oriented fibres contain ribbon-like micelles about 25[degree]A thick with their longest dimension parallel to the fibre axis. The ribbons are packed face to face with a variable interfacial separation around a mean of 15 [plus or minus] 4 A. The inner structure of the ribbons is basically that of the Tussah silk model as described by Marsh, Corey & Pauling (1955), but in the cross- P conformation the extended parts of the polypeptide chains run at right angles to the fibre axis. In the protein studied these extended parts are linked together by short "bend" regions to form continuous folded polypeptide chains which lie in planes normal to the surface of the ribbon-like micelles and parallel to their long axis.