The formation of a quaternary structure by recombinant analogs of spider silk proteins

被引：7

作者：

Sokolova, O. S. ^{[1
]}

Bogush, V. G. ^{[2
]}

Davydova, L. I. ^{[2
]}

Polevova, S. V. ^{[1
]}

Antonov, S. A. ^{[1
]}

Neretina, T. V. ^{[3
]}

Klinov, D. V. ^{[3
]}

Debabov, V. G. ^{[2
]}

Kirpichnikov, M. P. ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, Dept Biol, Moscow 119991, Russia

[2] State Res Ctr GosNIIGenet, Moscow 113545, Russia

[3] Russian Acad Sci, Shemyakin & Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

来源：

MOLECULAR BIOLOGY | 2010年 / 44卷 / 01期

基金：

俄罗斯基础研究基金会;

关键词：

recombinant proteins; spidroins; scanning electron microscopy; transmission electron microscopy; microfibers; DRAGLINE SILK; DESIGN; FIBERS;

D O I：

10.1134/S0026893310010188

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The morphology of the fibers formed by recombinant analogs of dragline spider silk proteins, spidroins 1 and 2, was studied. It has been shown that the extension of the initial fiber, the so-called as-spun fiber, leads to remodeling of the spongy matrix with the formation of microfibers, which is accompanied by a decrease in the fiber diameter. The breaking strength of the fiber depends not only on the primary structure of the constituent protein, but also on the way it was formed. Simulation of the assembly of microfibers and the fibers formed of them can clarify the natural spider web spinning and enhance the development of technology for producing biomaterials with unique properties.

引用

页码：150 / 157

页数：8

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