【摘要】 建立一种解析还原法羽毛再生材料中蛋白质二级结构差异的方法。对降解所得不同形式角蛋白再生物进行傅里叶变换红外光谱的测试,通过对其酰胺III带的分析,确定在羽毛的再生过程中所得的两种不同形式的降解物(角蛋白溶液和角蛋白凝胶)的二级结构的差异。实验证明:在角蛋白溶液中,α-螺旋占优势,含量在β-折叠之上;而在角蛋白凝胶物中,β-折叠占优势,说明这种结构的角蛋白分子之间更容易生成氢键等物理交联,在一定的环境条件,促使形成致密的角蛋白交联物。该法快速、有效、稳定和敏感,适用于检测还原法羽毛角蛋白再生材料二级结构。更多还原

【Abstract】 A method was established for identifying the secondary structure’s distinction of keratin regeneration materials obtained by reduction. In this study, through the analysis of two kinds of different forms of keratin in Fourier transform infrared spectroscopy testing and amide III belt,we can know the secondary structure’s distinction of keratin regeneration materials(keratin solution,keratin solution). Experiments show that in keratin solution,alpha helix predominates,content on beta fold; In keratin jello,beta folding edge,illustrates the structure of keratin easier to produce hydrogen bond between molecules such as physical crosslinking, in certain environmental conditions,to form a dense keratin crosslinking. This method is effective,stable,high sensitive. It is suitable for identifying the secondary structure’s distinction of keratin regeneration materials obtained by reduction更多还原