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FIU Electronic Theses and Dissertations

BPTI

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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Folding Analysis Of Reduced Bovine Pancreatic Trypsin Inhibitor (Bpti) With Aromatic Thiols And Disulfides In Vitro, Na Zhang Nov 2018

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 ...


Investigating The In Vitro Oxidative Folding Pathways Of Bovine Pancreatic Trypsin Inhibitor (Bpti), Yingsong Wang Nov 2013

Investigating The In Vitro Oxidative Folding Pathways Of Bovine Pancreatic Trypsin Inhibitor (Bpti), Yingsong Wang

FIU Electronic Theses and Dissertations

The oxidative folding pathway of the disulfide containing protein bovine pancreatic trypsin inhibitor (BPTI) was one of the first to be elucidated and has served as a basis for understanding the folding pathways of other proteins. During the oxidative folding of reduced BPTI, two intermediates (N' and N*) accumulate in significant amounts and act as kinetic traps. Both N' and N* bury their two remaining free thiols in their hydrophobic cores, which inhibits further oxidation. Historically, the rate limiting step was considered to be the intramolecular rearrangements of N' and N* to another intermediate with two free thiols, NSH ...