The folding of proteins that contain disulfide bonds is termed oxidative protein folding. It involves a chemical reaction resulting in the formation of disulfide bonds and a physical conformational folding reaction that promotes the formation of the native structure. While the presence of disulfide bonds significantly increases the complexity of the folding landscape, it is generally recognized that native disulfide bonds help funnel the trajectory towards the final folded form. Here, we review the role of disulfide bonds in oxidative protein folding and argue that even structure-inducing native disulfide bond formation treads a fine line in the regeneration of disulfide-bond-containing proteins. The translation of this observation to protein misfolding related disorders is discussed.

含有二硫键的蛋白质折叠称为氧化蛋白质折叠。它涉及导致形成二硫键的化学反应和促进天然结构形成的物理构象折叠反应。虽然二硫键的存在显着增加了折叠景观的复杂性，但人们普遍认为天然二硫键有助于将轨迹汇集到最终折叠形式。在这里，我们回顾了二硫键在氧化蛋白质折叠中的作用，并认为即使是结构诱导的天然二硫键形成在含二硫键的蛋白质的再生中也是一条细线。讨论了这一观察到蛋白质错误折叠相关疾病的转化。