Two distinct β-sheet fibrils from silk protein

被引：99

作者：

Gong, Zuguang ^{[2
]}

Huang, Lei ^{[2
]}

Yang, Yuhong ^{[1
]}

Chen, Xin ^{[2
]}

Shao, Zhengzhong ^{[2
]}

机构：

[1] Fudan Univ, Res Ctr Anal & Measurement, Shanghai 200433, Peoples R China

[2] Fudan Univ, Key Lab Mol Engn Polymers, Minist Educ, Adv Mat Lab,Dept Macromol Sci, Shanghai 200433, Peoples R China

来源：

CHEMICAL COMMUNICATIONS | 2009年 / 48期

关键词：

AMYLOID-LIKE FIBRILS; SOLID-STATE NMR; SPIDER SILK; RAMAN-SPECTROSCOPY; FIBER DIFFRACTION; FIBROIN; CONFORMATION; POLYMORPHISM; ORIENTATION; BINDING;

D O I：

10.1039/b914218e

中图分类号：

O6 [化学];

学科分类号：

070301 [无机化学];

摘要：

kThis study showed that Bombyx mori silk protein could be selectively induced to fold into fibrils dominated by either cross- or parallel-beta-sheet structure, where the beta-strands arrange perpendicular or parallel to the long fibril axis, incubated in ethanol-water quiescently or in water under shear.

引用

页码：7506 / 7508

页数：3

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