Bryant C, Strottmann J M, Stellwagen E
Biochemistry. 1985 Jul 2;24(14):3459-64. doi: 10.1021/bi00335a011.
A covalent dimer of Saccharomyces cerevisiae iso-1 cytochrome c is stabilized by an interchain disulfide bond involving the cysteine residue penultimate to the C-terminus. The individual chains in the dimer appear to retain the tertiary structural features characteristic for monomeric cytochrome c albeit with some perturbation. The dimer is reversibly denatured by heat, urea, or guanidine hydrochloride in a single cooperative transition whose midpoint is less than that of the monomeric protein. The kinetic profile observed for the refolding of the denatured dimer is characteristic for monomeric cytochromes except for a markedly enhanced slow-phase amplitude.
酿酒酵母同工酶-1细胞色素c的共价二聚体通过涉及C末端倒数第二个半胱氨酸残基的链间二硫键得以稳定。二聚体中的各个链似乎保留了单体细胞色素c特有的三级结构特征，尽管存在一些扰动。二聚体在单一协同转变中可被热、尿素或盐酸胍可逆变性，其转变中点低于单体蛋白。除了慢相振幅明显增强外，变性二聚体复性时观察到的动力学曲线是单体细胞色素的特征。
