Latypov R F, Dolgikh D A, Kirpichnikov M P, Ptitsyn O B, Roder H
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
Biofizika. 2001 Jan-Feb;46(1):46-52.
Equilibrium unfolding experiments on several mutant forms of horse heart cytochrome c were performed. By means of absorbance spectroscopy, the accumulation of an equilibrium intermediate was revealed upon unfolding of Y97V mutant protein, and its structural properties were characterized. The data obtained allow one to conclude that the equilibrium intermediate corresponds to the earliest kinetic intermediate Ic in cytochrome c folding reaction. A comparative analysis of spectral properties of unfolded states of cytochrome c induced by urea or guanidine hydrochloride is presented.
对马心细胞色素c的几种突变形式进行了平衡去折叠实验。通过吸光光谱法，发现Y97V突变蛋白去折叠时会积累一种平衡中间体，并对其结构特性进行了表征。所获得的数据使人们能够得出结论，该平衡中间体对应于细胞色素c折叠反应中最早的动力学中间体Ic。本文对尿素或盐酸胍诱导的细胞色素c未折叠状态的光谱特性进行了比较分析。
