35th Annual Student Research Conference
Investigation into Higher Ratios of DBF Compared to Denatured Lysozyme to Determine the Chaperone Activity of DBF
Corbin A. Estes
Dr. Cassidy Dobson, Faculty Mentor
Disulfide Bond Forming Enzyme (DBF) is a unique chaperone protein found in the hyperthermophile Sulfolobus solfataricus. DBF has the ability to chaperone disulfide bonds without the presence of cysteine, which separates it from other disulfide chaperones, implying a novel mechanism of action. DBF is overexpressed in E. coli, purified by immobilized metal affinity column chromatography, and analyzed via SDS-PAGE. One determines DBF activity by how well it acts as a molecular chaperone. By measuring the activity of refolded lysozyme by UV-Vis spectroscopy in the presence of DBF, one can monitor the ability of DBF to correctly refold disulfide bonds. In order to understand DBF’s unique mechanism, we are interested if a higher ratio of DBF to denatured lysozyme is able to refold disulfide interactions.
Keywords: Biochemistry, Disulfide Bond Forming Enzyme (DBF), Lysozyme Assays, Chaperone
Topic(s):Biochemistry and Molecular Biology
Chemistry
Presentation Type: Asynchronous Virtual Presentation
Session: 3-11
Location: https://flipgrid.com/d54e4a1e
Time: 0:00