Submission Date

7-19-2019

Document Type

Paper- Restricted to Campus Access

Department

Chemistry

Faculty Mentor

Amanda Reig

Student Contributor

Joe Pantel

Comments

Presented during the 21st Annual Summer Fellows Symposium, July 19, 2019 at Ursinus College.

Project Description

In nature, enzymes utilize metals to assist with various forms of catalysis. The De Novo Due Ferri Single Chain (DFsc) protein is a computationally designed four bundle helix model protein that mimics the active site of binuclear metalloenzymes. One of the many metal ions that can interact with the DFsc protein is Zinc, which is capable of hydrolase/nuclease activity. The goal of this project is to investigate the hydrolase/nuclease activity of zinc bound DFsc proteins. Several DFsc proteins were created with variations in the amino acids in the active site. These proteins were purified by HPLC. Nuclease activity was determined using DNA cleavage assays using both plasmid and linear DNA. Preliminary results indicate cleavage activity of both the DYG4DFsc protein and the G4DFsc protein.

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