Secondary structural analysis in the solid state for analogous sequential polypeptides of glycine-rich sequence of spider dragline silk

被引：12

作者：

Fukushima, Y ^{[1
]}

机构：

[1] Toyo Univ, Fac Engn, Dept Appl Chem, Kawagoe, Saitama 3508585, Japan

来源：

POLYMER BULLETIN | 2000年 / 45卷 / 03期

关键词：

D O I：

10.1007/s002890070026

中图分类号：

O63 [高分子化学（高聚物）];

学科分类号：

070305 ; 080501 ; 081704 ;

摘要：

Four sequential copolypeptides poly(X-Gly-Gly) with X being Ala, Tyr, Gln, or Leu were prepared as a model of glycine-rich sequence of dragline spider silk produced by Nephila clavipes and their secondary structures in the solid state were characterized by FT-IR spectroscopy. Poly(Tyr-Gly-Gly), poly(Gln-Gly-Gly), and poly(Ala-Gly-Gly) form the beta -sheet structures, whereas poly(Leu-Gly-Gly) existed as a disordered conformation as a cast film from formic acid. These results indicated that X-Gly-Gly sequences with Tyr, Gin, and Ala could contribute to the formation of the beta -sheet structure in glycine-rich sequence.

引用

页码：237 / 244

页数：8

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