Creighton T E
European Molecular Biology Laboratory, London, UK.
Biol Chem. 1997 Aug;378(8):731-44. doi: 10.1515/bchm.1997.378.8.731.
Protein folding that is coupled to disulphide bond formation has many experimental advantages. In particular, the kinetic roles and importance of all the disulphide intermediates can be determined, usually unambiguously. This contrasts with other types of protein folding, where the roles of any intermediates detected are usually not established. Nevertheless, there is considerable confusion in the literature about even the best-characterized disulphide folding pathways. This article attempts to set the record straight.
与二硫键形成相偶联的蛋白质折叠具有许多实验优势。特别是，所有二硫键中间体的动力学作用和重要性通常都能明确确定。这与其他类型的蛋白质折叠形成对比，在其他类型的蛋白质折叠中，所检测到的任何中间体的作用通常都未明确。然而，即使是关于特征最明确的二硫键折叠途径，文献中也存在相当大的混淆。本文试图澄清事实。
