32nd Annual Student Research Conference
Investigating the Molecular Mechanism of DBF Enzymes from Sulfolobus Solfataricus Archaebacteria as a Molecular Chaperone
Alyssa A. Tipler
Dr. Cassidy Dobson, Faculty Mentor
Disulfide bonds play a crucial role in the structure of proteins. Improperly folded proteins caused by incorrect disulfide bond formation can lead to a plethora of diseases, such as cataracts, ALS, and Parkinson’s Disease. Molecular chaperones assist with proper protein folding in the Endoplasmic Reticulum (ER). These chaperones such as Protein Disulfide Isomerase and Thioredoxin rearrange disulfides in a protein by using their intrinsic cysteine residues. Disulfide Bond Forming Enzyme (DBF) is a known disulfide bond chaperone capable of rearranging incorrect disulfides in the absence of cysteines. To investigate the mechanism of action of DBF we are using lysozyme as a model system due to the presence of disulfide bonds. By denaturing lysozyme and adding DBF we can observe its ability to refolded incorrectly made disulfides and then further investigate the mechanism by mutations of DBF.
Keywords: DBF, disulfide bond, molecular chaperone, lysozyme, misfolded protein, cataracts, cysteine, neurodegenerative
Topic(s):Biochemistry and Molecular Biology
Biology
Chemistry
Presentation Type: Oral Paper
Session: 108-4
Location: MC 209
Time: 9:15