Determining the mechanism by which proteins attain their native structure is an important but difficult problem in basic biology. The study of protein folding is difficult because it involves the identification and characterization of folding intermediates that are only very transiently present. Disulfide bond formation is thermodynamically linked to protein folding. The availability of thiol trapping reagents and the relatively slow kinetics of disulfide bond formation have facilitated the isolation, purification, and characterization of disulfide-linked folding intermediates. As a result, the folding pathways of several disulfide-rich proteins are among the best known of any protein. This review discusses disulfide bond formation and its relationship to protein folding in vitro and in vivo.

中文翻译：

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二硫键连接的蛋白质折叠途径。

在基本生物学中，确定蛋白质达到其天然结构的机制是一个重要但困难的问题。蛋白质折叠的研究很困难，因为它涉及鉴定和表征仅短暂存在的折叠中间体。二硫键的形成在热力学上与蛋白质折叠有关。硫醇捕集试剂的可用性和相对缓慢的二硫键形成动力学已经促进了二硫键连接的折叠中间体的分离，纯化和表征。结果，几种富含二硫键的蛋白质的折叠途径是所有蛋白质中最著名的。这篇综述讨论了二硫键的形成及其与体内外蛋白质折叠的关系。