36th Annual Student Research Conference
Using Disulfide Bond Forming Enzyme to Prevent or Correct Gamma-D Crystallin Aggregation
Karissa P. Williams
Dr. Cassidy Dobson (Colorado State University- Pueblo) and Dr. Stuart Winikoff, Faculty Mentors
Gamma crystallins are a class of proteins responsible for providing structure within the eye lens and contain disulfide bonds. When these disulfide bonds are improperly folded, protein aggregation occurs and cataracts form. 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 was chosen as an optimal disulfide chaperone as it possesses unique attributes including an atypical mechanism, absence of sulfur residues, and ability to refold disulfide bonds. Determination of the optimal aggregation conditions for Gamma-D Crystallin is crucial in order to test the functionality of DBF. To induce aggregation chemical oxidizing agents were added to a stock of protein and incubated. Size Exclusion Chromatography (SEC) will be used to quantitatively determine the impact of DBF on Gamma-D Crystallin aggregation.
Keywords: Disulfide bond-forming enzyme, protein aggregation, Gamma-D Crystallin, Size Exclusion Chromatography
Topic(s):Biochemistry and Molecular Biology
Presentation Type: Oral Presentation
Session: 308-1
Location: MG 1000
Time: 1:15