Honors Theses
Date of Award
Spring 5-10-2023
Document Type
Undergraduate Thesis
Department
Chemistry and Biochemistry
First Advisor
Saumen Chakraborty
Second Advisor
Vignesh Sundaresan
Third Advisor
Kensha Clark
Relational Format
Dissertation/Thesis
Abstract
Copper enzymes are found in nature. Their mechanisms and properties are unknown, as spectroscopy is limited. By creating artificially designed copper peptides through de novo design, the behavior, characteristics, and spectroscopy of copper enzymes can be studied to enhance understanding of the mechanisms involved with enzyme catalysis. Design, synthesis, purification, and characterization are completed to create a quality peptide mutant that can be studied to learn about natural enzymes. This plays an important role in pharmaceutical research, renewable energy sourcing, and studies of biological processes in the body. In this study, 3SCC de novo peptide is mutated at different positions, from Ile to Ala, to open the copper active site, allowing for more efficient binding and catalytic activity. Electrochemical and kinetic experiments are currently being conducted to measure catalytic activity at different temperatures to ultimately find the reorganization energy, ��, of the 3SCC and mutants.
Recommended Citation
Murphy, Morgan, "De Novo Design of Artificial Cu Peptide for Substrate Oxidation and an Electrochemical Approach to Determine Reorganization Energy" (2023). Honors Theses. 2857.
https://egrove.olemiss.edu/hon_thesis/2857
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