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利用Fourier红外光谱对二硫键完整和还原的核糖核酸酶A(RNase A),牛血清白蛋白(BSA)和溶菌酶在6mol/L盐酸胍中变性后的结构进行了比较。这三种蛋白质,在二硫键完整和还原状态下变性后的Fourier红外酰胺Ⅰ带光谱都表现了不同程度的差异,但是三种还原蛋白质在完全变性后的光谱却非常相似。说明含有完整天然二硫键的蛋白在6mol/L盐酸胍中变性后仍然有相当程度的残留有序结构,而二硫键断开的蛋白质完全变性后在结构上却是相似的。
Fourier transform infrared spectroscopy (FTIR) was used to compare the structure of RNase A, bovine serum albumin (BSA) and lysozyme modified by disulfide bond in 6 mol / L guanidine hydrochloride. The three bands of Fourier transform infrared spectra of these three proteins, both denatured and disulfide bond intact and reduced, showed different degrees of difference, but the spectra of the three reduced proteins after complete denaturation were very similar. Indicating that proteins containing intact natural disulfide bonds still have a considerable degree of residual ordered structure after being denatured in 6 mol / L guanidine hydrochloride, whereas proteins disrupted by disulfide bonds are structurally similar after denaturation.