Submission Date
7-22-2022
Document Type
Paper- Restricted to Campus Access
Department
Biochemistry & Molecular Biology
Faculty Mentor
Amanda Reig
Project Description
The de novo Due Ferri Single Chain protein model has been shown to be a viable protein scaffold to study functional characteristics through its thermodynamically favored and structurally sound four-helix bundle motif. Previous studies have shown that DFsc proteins exhibit DNA cleavage activity in time-controlled experiments. Additionally, phosphate bond cleavage activity has been demonstrated through small molecule studies using bis-4-nitrophenylphosphate (BNPP) cleavage assays. In this study, the metal binding equivalencies in several DFsc proteins was determined as well as their phosphatase activity using 6,8-difluoro-4-methylumbelliferyl phosphate (difMUP) fluorescence absorption spectroscopy assays.
Recommended Citation
Goldschmidt, Avraham, "Small Molecule Phosphatase Activity and Metal Binding Equivalencies of De Novo Due Ferri Single Chain Proteins" (2022). Biochemistry and Molecular Biology Summer Fellows. 25.
https://digitalcommons.ursinus.edu/biochem_sum/25
Restricted
Available to Ursinus community only.
Comments
Presented during the 24th Annual Summer Fellows Symposium, July 22, 2022 at Ursinus College.
This research was funded by a grant from the National Institutes of Health (Grant# R15-GM114906).