Mechanisms of oxidative protein folding in the periplasm of E. coli

半胱氨酸对之间形成的二硫键对许多分泌蛋白和膜蛋白的折叠、活性和稳定性都很重要。在大肠杆菌中，一种叫做DsbA的酶将二硫键引入到周围质中折叠的蛋白质中。在本研究中，我在体内检测了DsbA与其底物之间形成二硫键的中间体。对中间体的详细描述揭示了一些关于这个细胞区室中蛋白质折叠的新见解。

Disulfide bonds, formed between pairs of cysteines, are important for the folding,activity, and stability of many secretory and membrane proteins. In a bacterium Escherichia coli, an enzyme called DsbA introduces disulfide bonds into folding proteins in the periplasm. In this study, I detected, in vivo, the intermediates of disulfide bond formation that were formed between DsbA and its substrates. Detailed characterization of the intermediates revealed a number of new insights into protein folding in this cellular compartment.