35th Annual Student Research Conference
Mutagenesis of Disulfide Bond Forming Enzyme
Leah M. Chaney
Dr. Cassidy Dobson, Faculty Mentor
The formation of crystallin protein aggregates can arise due to improperly folded disulfide bonds. Aggregations of these proteins are known to cause cataracts, the leading cause of blindness in the world. Disulfide Bond Forming (DBF) Enzyme acts as a chaperone protein to correct misfolded disulfide bonds in crystallin proteins. As a chaperone, DBF is unique in that it does not contain sulfur residues or follow the typical mechanism of disulfide chaperones, such as Thioredoxins. DBF is the only protein in the Sso7d family that is known to possess the ability to refold disulfide bonds. A valine in the 59th position is one of the main differences between other proteins within the Sso7d family and the sequence of DBF. In order to ultimately determine the mechanism of DBF’s disulfide refolding capabilities, the role of V59 was investigated by mutating valine into glutamic acid, arginine, tryptophan, and glutamine through PCR mutagenesis.
Keywords: PCR Mutagenesis, Disulfide Bonds, Aggregation, Chaperone
Topic(s):Biochemistry and Molecular Biology
Chemistry
Biology
Presentation Type: Oral Presentation
Session: 106-1
Location: MG 1000
Time: 8:30