Biochemistry, Biophysics, and Structural Biology Commons^™

Folding Analysis Of Reduced Bovine Pancreatic Trypsin Inhibitor (Bpti) With Aromatic Thiols And Disulfides In Vitro, Na Zhang

FIU Electronic Theses and Dissertations

Almost all therapeutic proteins contain disulfide bonds to stabilize their native structure. Recombinant DNA technology enables many therapeutic proteins to be produced in bacteria, but the expression of native proteins is not always efficient due to the limited ability of bacteria to form disulfide bonds in vivo. It is often necessary to employ in vitro oxidative folding process to form the native disulfide bonds to obtain the native structure of disulfide-containing proteins. Aromatic disulfides are small molecules designed to match some of the physical properties of the active site of protein disulfide isomerase (PDI), which catalyzes the folding process of …