Submission Date

7-22-2022

Document Type

Paper- Restricted to Campus Access

Department

Biochemistry & Molecular Biology

Faculty Mentor

Amanda Reig

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).

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.

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