溶菌酶水溶液的激光拉曼谱

The Raman Spectra of the Lysozyme in Aqueous Solution

本文报道了溶菌酶水溶液的激光拉曼谱。酰胺Ⅰ振动谱带在1657cm^(-1),酰胺Ⅱ振动谱带在1302和1253cm^(-1),酪氨酸残基的特征谱带在854和837cm^(-1)。硫—硫桥键的振动谱带在505cm^(-1)。并由此定性地证明了该蛋白质分子的肽链主要由α—螺旋和无规则卷曲组成,酪氨酸残基在分子中呈三分之二“暴露”式,硫—硫键部位的几何构型为扭式—扭式—扭式。

The Raman Spectra of the lysozyme in aqueous solution have been studied.Theamide Ⅰ band appears at 1657 cm^(-1),amide (?) band appears at 1302 and 1253 cm^(-1).Thecharacteristic Raman bands of the tyrosine residue are at 854 and 837 cm^(-1).The band of theS—S band is at 505cm^(-1).All the characteristic Raman bands of this protein prove that itsstructure consists of the α-helix and random coil.The tyrosine residue is“exposed”in itstwo thirds.The conformation of the Carbon atoms in the disulfide bridge C—C—S—S—C—C is gauche—gauche-gauche.