Document Type

Paper- Restricted to Campus Access

Publication Date


Faculty Mentor

Amanda Reig


We are investigating the electrochemical properties of the protein that we currently use in our laboratory and its variants. The due ferri single chain (DFsc) protein is a de novo designed four-helix bundle designed to mimic the 2-His/4-carboxylate active site of natural non-heme di-iron enzymes. In order to better understand the structure-function relationship of these variants, the reduction-oxidation properties of these di-iron proteins were probed using cyclic voltammetry. With the electrochemistry, we are looking to better understand the oxidation reduction properties of the protein since this is what makes metalloproteins unique with its metal complexes bound within the helices to stabilize and perform redox reactions. This semester, we specifically looked at the effect of pH on our proteins. If we are able to better understand our proteins and its ability to effectively carry out redox reactions, like ones in nature, we could be able to apply this to better understanding their importance and function in biological processes. This could allow for artificial design of proteins for modern applications such as biosensors and catalysts.


Presented as part of the Ursinus College Celebration of Student Achievement (CoSA) held April 23 – April 30, 2020.

The downloadable file is a PowerPoint slide presentation with recorded audio commentary.

Audio run time is approximately 5 minutes.

This research was also submitted to the Spring 2020 American Chemical Society Expo.


Available to Ursinus community only.