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

两对半胱氨酸之间形成的二硫键对许多分泌型和膜型蛋白质的折叠、活性和稳定性都很重要。在细菌大肠杆菌中，一种名为DsbA的酶将二硫键引入周质中的折叠蛋白质中。在这项研究中，我在体内检测到了在DsbA及其底物之间形成二硫键的中间产物。对中间产物的详细表征揭示了对这个细胞隔间中蛋白质折叠的一些新的见解。

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.