34th Annual Student Research Conference
Qualitative Study of the Chaperone Activity of DBF Enzyme on Protein Aggregates
Guthrie L. Stroh
Dr. Cassidy Dobson, Faculty Mentor
Disulfide Bond-Forming enzyme (DBF) is a small molecular chaperone protein isolated from the extremophilic archaebacterium Sulfolobus solfataricus. DBF has the unique ability to rearrange disulfide bonds without itself containing the cysteine residue(s) quintessential to similarly functioning chaperones. In order to elucidate this idiosyncratic structure, it is first important to study the effectiveness of DBF to refold protein aggregates (incorrectly folded clusters held together by disulfide bonds). Protein aggregates are causal of many diseases such as cataracts and Alzheimer’s, so a protein like DBF could have significant medical application. DBF’s activity will be studied through lysozyme assays, which will test the ability of DBF to refold denatured lysozyme under various environmental conditions in vitro through UV-Vis spectrophotometry. These test cases then will be compared to positive and negative controls. The DBF protein has previously been recombinantly expressed in E.Coli cells, then purified and concentrated in preparation for experimentation.
Keywords: Disulfide Bond-Forming enzyme, protein aggregates, lysozyme assay, chaperone proteins, disulfide bonds, re-folding
Topic(s):Biochemistry and Molecular Biology
Chemistry
Biology
Presentation Type: Asynchronous Virtual Oral Presentation
Session: 3-13
Location: https://flipgrid.com/f86d186b
Time: 0:00