【摘 要】
：
The molecular conformations of four silk fibroin crystalline analogues[GAGAG-JT]16 ( G, Gly; A, Ala; J = Ala. Ser, Tyr or Val, designated eGA, eGS, eGY or eGV)
【机 构】
：
National Engineering Laboratory for Modern Silk,College of Textile and Clothing Engineering
论文部分内容阅读
The molecular conformations of four silk fibroin crystalline analogues[GAGAG-JT]16 ( G, Gly; A, Ala; J = Ala. Ser, Tyr or Val, designated eGA, eGS, eGY or eGV) , carried out using molecular design and expressed by Escherichia coil ( E. coli) , were evaluated by Raman spectra analysis. The abilities of forming β-sheet structure were determined by thioflavin T( ThT) fluorescence spectra analysis. In terms of molecular conformation, except eGY that could not form significant typical molecular conformation, eGS and eGV were mainly composed of p-sheets while eGA tended to form β-turn. β-turn was also present in eGY and absent in eGS and eGV. In terms of β-sheet structure, eGS had the highest β-sheet content, followed by eGV, and eGA had the lowest content, furthermore, β-sheet structures were more stable in eGS and eGV than those in eGA and eGY.
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