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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The zipper groups of the amyloid state of proteins
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The zipper groups of the amyloid state of proteins

机译:拉链的淀粉样蛋白的蛋白质

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Fibrous proteins in the amyloid state are found both associated with numerous diseases and in the normal functions of cells. Amyloid fibers contain a repetitive spine, commonly built from a pair of β-sheets whose β-strands run perpendicular to the fiber direction and whose side chains interdigitate, much like the teeth of a zipper. In fiber spines known as homosteric zippers, identical protein segments sharing identical packing environments make the two β-sheets. In previous work based on atomic resolution crystal structures of homosteric zippers derived from a dozen proteins, the symmetries of homosteric zippers were categorized into eight classes. Here, it is shown through a formal derivation that each homosteric zipper class corresponds to a unique set of symmetry groups termed 'zipper groups'. Furthermore, the eight previously identified classes do not account for all of the 15 possible zipper groups, which may be categorized into the complete set of ten classes. Because of their foundations in group theory, the 15 zipper groups provide a mathematically rigorous classification for homosteric zippers.
机译:纤维状蛋白质淀粉样状态与多种疾病相关的和细胞的正常功能。一个重复的脊椎,通常由一对β床单的β链垂直于运行纤维方向,其侧链互相交叉,就像一个拉链的牙齿。在纤维刺称为homosteric拉链,相同的蛋白质片段分享相同的包装环境使两个β片。以前的工作基于原子分辨率晶体homosteric拉链结构源于一个打蛋白,homosteric的对称性拉链是分为八类。这里,它显示通过正式的推导每个类对应于homosteric拉链一组独特的对称组称为“拉链组”。确定不占所有的类15可能拉链团体分为十类的完整。在组织理论中,因为他们的基础15拉链集团提供一个数学严格分类homosteric拉链。

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