35th Annual Student Research Conference
Using Disulfide Bond Forming Enzyme to Prevent Gamma-D Crystallin Aggregation
Karissa P. Williams
Dr. Cassidy Dobson, Faculty Mentor
Gamma crystallins are a class of proteins that provide structure within the lens of the eye and contain cysteines which form disulfide bonds. When these disulfide bonds are improperly paired, protein aggregation occurs which can lead to the formation of cataracts. Our lab is currently investigating if the molecular chaperone protein Disulfide Bond Forming Enzyme (DBF) possesses the ability to prevent or correct disulfide-mediated aggregates in Gamma-D Crystallin. DBF possesses the ability to rearrange disulfide bonds even though the protein itself lacks cysteine residues, making it distinguishable from all other disulfide chaperones. In order to determine if DBF is capable of preventing or reversing disulfide-mediated aggregates, our lab is inducing disulfide mediated aggregation and using Size Exclusion Chromatography (SEC) to observe the changes in Gamma-D Crystallin aggregation status with and without DBF.
Keywords: Disulfide Bond Forming Enzyme (DBF), protein aggregation, Gamma-D Crystallin, disulfide bonds, Size Exclusion Chromatography (SEC)
Topic(s):Biochemistry and Molecular Biology
Presentation Type: Oral Presentation
Session: 305-4
Location: MG 2001
Time: 2:00