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The Molecular Mechanism of Spider-Silk Formation

机译:蜘蛛丝形成的分子机理

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Spider silk, one of the most remarkable biomaterials, is made of fibers whose mechanical properties exceed those of steel once the smaller density of spider silk is taken into account: A spider silk fiber spun around the earth's equator would weigh not more than 500 grams. Spider silk from Araneus diadematus spiders contains a polypeptide chain consisting of a so-called AQ repeat sequence of low complexity in its composition (A, hydrophobic polyalanine-rich motif: GPYGPGASA6GGYGPGSGQQ; Q, hydrophilic glutamine-and glycine-rich motif: (GPGQQ)4). The repeat sequence is a central part of the fiber and its role is reminiscent of the repeat sequence in collagen. Twelve AQ sequences are flanked by a secretion signal, along with non-repetitive N-and C-terminal domains, each of which is implicated in a number of different functions, including control of solubility and fiber formation.
机译:蜘蛛丝是最杰出的生物材料之一,由纤维制成,一旦考虑到密度较小的蜘蛛丝,其机械性能就会超过钢:围绕地球赤道旋转的蜘蛛丝纤维的重量不超过500克。来自Araneus diadematus蜘蛛的蜘蛛丝含有一条多肽链,该多肽链由其组成复杂度低的所谓AQ重复序列组成(A,疏水性富含聚丙氨酸的基序:GPYGPGASA6GGYGPGSGQQ; Q,亲水性富含谷氨酰胺和甘氨酸的基序:(GPGQQ) 4)。重复序列是纤维的中心部分,其作用让人联想到胶原蛋白中的重复序列。十二个AQ序列旁有一个分泌信号,以及非重复的N和C端结构域,每个结构域都涉及许多不同功能,包括对溶解度和纤维形成的控制。

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