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本文引用的文献

1
Elasticity of spider silks.蜘蛛丝的弹性。
Biomacromolecules. 2008 Jul;9(7):1782-6. doi: 10.1021/bm7014174. Epub 2008 Jun 5.
2
The role of proline in the elastic mechanism of hydrated spider silks.脯氨酸在水合蜘蛛丝弹性机制中的作用。
J Exp Biol. 2008 Jun;211(Pt 12):1948-57. doi: 10.1242/jeb.014225.
3
The effect of proline on the network structure of major ampullate silks as inferred from their mechanical and optical properties.从脯氨酸的力学和光学性质推断其对主要壶腹丝网络结构的影响。
J Exp Biol. 2008 Jun;211(Pt 12):1937-47. doi: 10.1242/jeb.014217.
4
Properties of synthetic spider silk fibers based on Argiope aurantia MaSp2.基于金蛛属橙腹蛛MaSp2的合成蜘蛛丝纤维的特性
Biomacromolecules. 2008 Jun;9(6):1506-10. doi: 10.1021/bm701124p. Epub 2008 May 6.
5
Structural disorder in silk proteins reveals the emergence of elastomericity.丝蛋白中的结构紊乱揭示了弹性的出现。
Biomacromolecules. 2008 Jan;9(1):216-21. doi: 10.1021/bm701069y. Epub 2007 Dec 14.
6
Silk genes support the single origin of orb webs.丝蛋白基因支持圆网蛛的单一起源。
Science. 2006 Jun 23;312(5781):1762. doi: 10.1126/science.1127946.
7
Solid-state NMR analysis of a peptide (Gly-Pro-Gly-Gly-Ala)6-Gly derived from a flagelliform silk sequence of Nephila clavipes.对源自棒络新妇鞭状丝序列的肽（甘氨酸-脯氨酸-甘氨酸-甘氨酸-丙氨酸）6-甘氨酸进行固态核磁共振分析。
Biomacromolecules. 2006 Apr;7(4):1210-4. doi: 10.1021/bm0600522.
8
An investigation of the divergence of major ampullate silk fibers from Nephila clavipes and Argiope aurantia.对来自金蛛和横纹金蛛的主要壶腹状丝纤维的差异研究。
Biomacromolecules. 2005 Nov-Dec;6(6):3095-9. doi: 10.1021/bm050421e.
9
Scalable molecular dynamics with NAMD.使用 NAMD 的可扩展分子动力学
J Comput Chem. 2005 Dec;26(16):1781-802. doi: 10.1002/jcc.20289.
10
Altering the mechanics of spider silk through methanol post-spin drawing.通过甲醇后纺拉伸改变蜘蛛丝的力学性能。
Biomed Sci Instrum. 2005;41:1-6.

计算机模拟揭示模型MaSp1和MaSp2样肽对合成大壶腹丝纤维力学性能的不同贡献。

Distinct contributions of model MaSp1 and MaSp2 like peptides to the mechanical properties of synthetic major ampullate silk fibers as revealed in silico.

作者信息

Brooks Amanda E, Nelson Shane R, Jones Justin A, Koenig Courtney, Hinman Michael, Stricker Shane, Lewis Randolph V

机构信息

Department of Molecular Biology, University of Wyoming, Laramie, WY, USA.

出版信息

Nanotechnol Sci Appl. 2008 Aug 8;1:9-16. doi: 10.2147/nsa.s3961.

DOI:10.2147/nsa.s3961
PMID:20657704
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2908418/
Abstract

All characterized major ampullate silks from orb-web weaving spiders are composites of primarily two different proteins: MaSp1 and MaSp2. The conserved association of MaSp1 and MaSp2 in these spider species, the highly conserved amino acid motifs, and variable ratios of MaSp1 to MaSp2 demonstrate the importance of both MaSp1 and MaSp2 to the strength and elasticity of the fiber. Computer simulated mechanical tests predicted differing roles for MaSp1 and MaSp2 in the mechanical properties of the fibers. Recombinant MaSp1 and MaSp2 proteins were blended and spun into fibers mimicking the computer-simulated conditions. Mechanical testing verified the differing roles of MaSp1 and MaSp2.

摘要

所有已鉴定的圆网蛛主要壶腹丝均主要由两种不同蛋白质组成

MaSp1和MaSp2。在这些蜘蛛物种中，MaSp1和MaSp2的保守组合、高度保守的氨基酸基序以及MaSp1与MaSp2的可变比例表明，MaSp1和MaSp2对纤维的强度和弹性都很重要。计算机模拟力学测试预测了MaSp1和MaSp2在纤维力学性能中的不同作用。将重组MaSp1和MaSp2蛋白混合并纺成模仿计算机模拟条件的纤维。力学测试证实了MaSp1和MaSp2的不同作用。