Folding of Bovine Pancreatic Trypsin Inhibitor (BPTI) is Faster using Aromatic Thiols and their Corresponding Disulfides

Folding of Bovine Pancreatic Trypsin Inhibitor (BPTI) is Faster using Aromatic Thiols and their Corresponding Disulfides

Improvement in the in vitro oxidative folding of disulfide-containing proteins, such as extracellular and pharmaceutically important proteins, is required. Traditional folding methods using small molecule aliphatic thiol and disulfide, such as glutathione (GSH) and glutathione disulfide (GSSG) are s...

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Bibliographic Details
Main Author: Marahatta, Ram Prasad
Format: Others
Published: FIU Digital Commons 2017
Subjects:
Protein folding
glutathione (GSH)
glutathione disulfide (GSSG)
aromatic thiols
aromatic disulfides
BPTI
HPLC
molecular dynamics (MD)
Targeted MD (TMD)
conformational folding
Analytical Chemistry
Biological and Chemical Physics
Medicinal-Pharmaceutical Chemistry
Organic Chemistry
Online Access:https://digitalcommons.fiu.edu/etd/3530
https://digitalcommons.fiu.edu/cgi/viewcontent.cgi?article=4604&context=etd

Internet

https://digitalcommons.fiu.edu/etd/3530
https://digitalcommons.fiu.edu/cgi/viewcontent.cgi?article=4604&context=etd

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