Synthesis of aromatic monothiols to increase the folding rate and yields of disulfide-containing proteins
Document Type
Thesis
Degree
Master of Science (MS)
Major/Program
Chemistry
First Advisor's Name
Watson Lees
First Advisor's Committee Title
Committee Chair
Second Advisor's Name
David Chatfield
Third Advisor's Name
J. Martin E. Quirke
Date of Defense
7-15-2011
Abstract
Almost all pharmaceutically relevant proteins and many extracellular proteins contain disulfide bonds, which are essential for protein functions. In many cases, disulfidecontaining proteins are produced via in vitro protein folding that involves the oxidation of reduced protein to native protein, a complex process. The in vitro folding of reduced lysozyme has been extensively studied as a model system because native lysozyme is small, inexpensive, and has only four disulfide bonds. The folding of reduced lysozyme is conducted with the aid of a redox buffer consisting of a small molecule disulfide and a small molecule thiol, such as oxidized and reduced glutathione. Herein, in vitro folding rates and yields of lysozyme obtained in the presence of a series of aromatic thiols and oxidized glutathione are compared to those obtained with reduced and oxidized glutathione. Results showed that aromatic thiols significantly increase the folding rate of lysozyme compared to glutathione.
Identifier
FI14050441
Recommended Citation
Barrett, Elvis Jermaine, "Synthesis of aromatic monothiols to increase the folding rate and yields of disulfide-containing proteins" (2011). FIU Electronic Theses and Dissertations. 1409.
https://digitalcommons.fiu.edu/etd/1409
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