Submission Date
7-19-2024
Document Type
Paper- Restricted to Campus Access
Department
Chemistry
Second Department
Biochemistry & Molecular Biology
Faculty Mentor
Amanda Reig
Project Description
The DFsc protein, also known as the de novo protein, is a computer designed protein used to mimic metalloproteins in nature. With a structure of four alpha helices, this protein can bind to a multitude of metals ranging from zinc to titanium while also having the ability to oxidize small substrates and cleave DNA. The goal of the project is to mutate the original active site of the DFsc protein, changing a nearby isoleucine to aspartic acid (I100D) or glutamic acid (I100E). The negative charge of the carboxylate group should interact with the positive charge of the metals. These proteins will be created, purified, and then tested to see if changing the structure of the protein will affect its function. These tests include metal binding assays (iron, cobalt) using instruments such as UV-Vis spectroscopy.
Recommended Citation
Dunham-Snipes, Seth, "Mutations of the DFsc Protein Active Site" (2024). Biochemistry and Molecular Biology Summer Fellows. 30.
https://digitalcommons.ursinus.edu/biochem_sum/30
Restricted
Available to Ursinus community only.
Comments
Presented during the 26th Annual Summer Fellows Symposium, July 19, 2024 at Ursinus College.