Toniolo C, Fontana A, Scoffone E
Eur J Biochem. 1975 Jan 2;50(2):367-74. doi: 10.1111/j.1432-1033.1975.tb09812.x.
Ultraviolet absorption and circular dichroism studies have been carried out on horse heart apo-cytochrome c and heme-free peptide fragments obtained by cyanogen bromide cleavage of the native protein. It was noted that the various peptides assume predominantly an unordered conformation in water solution. Increasing ionic strength and addition of 2-chloroethanol increase the right-handed helical content. Guanidinium hydrochloride favors the coil state. It was also demonstrated that two non-interacting helical regions of different stability are present in the apo-protein in 2-chloroethanol.
对马心脱辅基细胞色素c以及通过溴化氰裂解天然蛋白质获得的无血红素肽片段进行了紫外吸收和圆二色性研究。注意到各种肽在水溶液中主要呈现无序构象。增加离子强度和添加2-氯乙醇会增加右手螺旋含量。盐酸胍有利于卷曲状态。还证明在2-氯乙醇中的脱辅基蛋白质中存在两个稳定性不同的非相互作用螺旋区域。
