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本文用紫外差光谱、紫外二阶导数光谱和圆二色光谱,对二硫键完整和经还原并氨酰羧甲基化(以下简称还原)的核糖核酸酶A(RNase A),牛血清白蛋白(BSA)和溶菌酶在6 mol/L盐酸胍中变性后的结构进行了比较。尽管在圆二色光谱中,二硫键完整和还原的变性蛋白都看不到α-螺旋和β-折叠等有序二级结构的存在,但是,与二硫键还原的变性蛋白相比,含有完整天然二硫键的变性蛋白在芳香族氨基酸残基侧链的暴露程度上明显较低。这些结果说明含有完整天然二硫键的蛋白在6mol/L盐酸胍中变性后可能仍然保留有一定程度的有序空间结构。
In this paper, the UV-vis, UV-second derivative spectra and circular dichroism spectra were used to analyze the relationship between disulfide bond integrity and reduced and aminoacylated carboxymethylation (RNase A), bovine serum albumin The structure of protein (BSA) and lysozyme denatured in 6 mol / L guanidine hydrochloride were compared. Although in the circular dichroism spectrum, disulfide bond intact and reduced denatured protein can not see the existence of ordered secondary structure such as α-helix and β-sheet, however, compared with the disulfide reduced denatured protein, The denatured protein containing an intact natural disulfide bond is significantly lower in the degree of side chain exposure of aromatic amino acid residues. These results indicate that proteins containing intact native disulfide bonds may still retain some degree of ordered spatial structure after denaturation in 6 mol / L guanidine hydrochloride.