各种蜘蛛牵引丝纤维的固态 NMR 比较。
Solid-state NMR comparison of various spiders' dragline silk fiber.
机构信息
Department of Molecular Biology and Macromolecular Core Facility, University of Wyoming, Laramie, Wyoming 82071, USA.
出版信息
Biomacromolecules. 2010 Aug 9;11(8):2039-43. doi: 10.1021/bm100399x.
Abstract
Major ampullate (dragline) spider silk is a coveted biopolymer due to its combination of strength and extensibility. The dragline silk of different spiders have distinct mechanical properties that can be qualitatively correlated to the protein sequence. This study uses amino acid analysis and carbon-13 solid-state NMR to compare the molecular composition, structure, and dynamics of major ampullate dragline silk of four orb-web spider species ( Nephila clavipes , Araneus gemmoides , Argiope aurantia , and Argiope argentata ) and one cobweb species ( Latrodectus hesperus ). The mobility of the protein backbone and amino acid side chains in water exposed silk fibers is shown to correlate to the proline content. This implies that regions of major ampullate spidroin 2 protein, which is the only dragline silk protein with any significant proline content, become significantly hydrated in dragline spider silk.
摘要
大型壶腹状（牵引丝）蜘蛛丝是一种令人垂涎的生物聚合物，因为它兼具强度和可拉伸性。不同蜘蛛的牵引丝具有明显不同的机械性能，可以定性地与蛋白质序列相关联。本研究使用氨基酸分析和碳-13 固态 NMR 来比较四种蛛网蜘蛛物种（Nephila clavipes、Araneus gemmoides、Argiope aurantia 和 Argiope argentata）和一种圆网蜘蛛物种（Latrodectus hesperus）的主要壶腹状牵引丝的分子组成、结构和动力学。暴露在水中的丝纤维中蛋白质主链和氨基酸侧链的流动性与脯氨酸含量相关。这意味着主要壶腹状丝蛋白 2 蛋白中富含脯氨酸的区域在牵引丝蜘蛛丝中会变得明显水合。
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