Date of Award

4-6-2018

Document Type

Honors Thesis

Department

Biology

First Advisor

Peter Lyons

Abstract

Enzymes must fold properly to function. For carboxypeptidases, a prodomain usually assists in this process. However, carboxypeptisdase 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.

Subject Area

Amino acids; Carboxypeptidases

Creative Commons License

Creative Commons Attribution-No Derivative Works 4.0 License
This work is licensed under a Creative Commons Attribution-No Derivative Works 4.0 License.

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