Poster Title
P-15 Critical Amino Acids for the Folding of Carboxypeptidase O
Abstract
Enzymes must fold properly to function. For carboxypeptidases, a prodomain usually assists in this process. However, carboxypeptidase O (CPO) can fold without one. We hypothesized that this prodigious ability could arise from an amino acid whose fortunate positioning stabilizes its neighbors during folding. We identified four unique, conserved amino acids and mutated them to their equivalent counterpart in CPA, a cousin of CPO, which requires a prodomain. We expressed the mutated genes in mammalian cells and checked for expression by western blotting. Our results indicate that three of four mutations were not expressed, hinting at the possible importance of these sites in the folding of CPO.
Start Date
3-2-2018 2:30 PM
P-15 Critical Amino Acids for the Folding of Carboxypeptidase O
Enzymes must fold properly to function. For carboxypeptidases, a prodomain usually assists in this process. However, carboxypeptidase O (CPO) can fold without one. We hypothesized that this prodigious ability could arise from an amino acid whose fortunate positioning stabilizes its neighbors during folding. We identified four unique, conserved amino acids and mutated them to their equivalent counterpart in CPA, a cousin of CPO, which requires a prodomain. We expressed the mutated genes in mammalian cells and checked for expression by western blotting. Our results indicate that three of four mutations were not expressed, hinting at the possible importance of these sites in the folding of CPO.
Acknowledgments
Dr. Peter Lyons.
J. N. Andrews Honors Program.
AU Office of Research & Creative Scholarship.