34th Annual Student Research Conference
Mutagenesis of Disulfide Bond Forming Enzyme
Reuben Kern
Dr. Cassidy Dobson, Faculty Mentor
Cataracts are caused by aggregation of crystallin proteins in the eye, and in some cases this misfolding is caused by incorrect disulfide bonding. Disulfide Bond Forming Enzyme (DBF) is a chaperone protein shown to rearrange and correct misfolded proteins to return them to their native state. In every other disulfide chaperone this reaction requires sulfurs internal to the chaperone, however DBF contains no sulfur residues and is unable to follow the typical mechanism. In order to elucidate the mechanism DBF uses to refold proteins, mutant versions of the protein need to be obtained. Using primers designed to replace one amino acid with another, DBF was mutated to four different residues. Comparing how efficient these variants are should determine the role of the original amino acid and contribute to our understanding of how DBF is able to conduct such a reaction.
Keywords: Mutagenesis, DBF, Protein, Chaperones, Molecular Biology
Topic(s):Biochemistry and Molecular Biology
Biology
Chemistry
Presentation Type: Asynchronous Virtual Oral Presentation
Session: 3-15
Location: https://flipgrid.com/f86d186b
Time: 0:00