Submission Date
4-25-2022
Document Type
Paper- Restricted to Campus Access
Department
Biochemistry & Molecular Biology
Adviser
Amanda Reig
Committee Member
Samantha Wilner
Committee Member
Hugo Montesinos-Yufa
Department Chair
Eric Williamsen
Department Chair
Anthony Lobo
Project Description
Metalloproteins are found in nature and involved in biological processes, especially in the cleavage of various molecular bonds. Of particular relevance are metallohydrolases, a class of enzymes that have the ability to catalyze hydrolysis by using water to break chemical bonds and using their metal cofactors to aid in this process. To better understand these natural enzymes, the de novo designed non-heme four-helix bundle Due Ferri single chain (DFsc) protein is used as a model system as it has a similar binuclear active site composition. The simpler structure of this model is helpful for studying the complex mechanism of DNA cleavage and better understand the protein’s structure-function relationship as a hydrolase. Here we investigated the ability of DFsc to cleave and linearize the pUC19 plasmid, changing different parameters, like metal cofactors and protein active site composition.
Recommended Citation
Huynh, Alana, "DNA Cleavage Activity of de novo Designed Due Ferri Single Chain (DFsc) Proteins" (2022). Biochemistry and Molecular Biology Honors Papers. 10.
https://digitalcommons.ursinus.edu/biochem_hon/10
Comments
This project was funded by the National Institutes of Health (NIH grant R15-GM144906-01).