Document Type

Paper- Restricted to Campus Access

Publication Date


Faculty Mentor

Samantha Wilner


Our goal is to better understand the unknown function of the structurally-known 3H04 protein from a biochemical perspective. The 3H04 protein is a small protein that has been expressed well in E. coli using a plasmid. The protein has been observed to be similar to many different naturally occurring proteins, including a hydrolase found in Staphylococcus aureus and an esterase; however, the protein itself has not been characterized well in the wet lab, so the exact function of this protein remains unknown. We used biochemical techniques to express, purify, and analyze the 3H04 protein to better understand its function and characteristics in the laboratory setting. The protein was purified using affinity chromatography. The molecular weight of the protein was determined as 73.4 kDa through SDS-PAGE and the concentration of purified protein was determined as 0.393 mg/mL by the Bradford assay. The kinetics of the protein were then determined using the pnitrophenyl acetate (PNPA) assay. Additionally, this assay allowed us to resolve whether or not 3H04 is a hydrolase.


Presented as part of the Ursinus College Celebration of Student Achievement (CoSA) held April 22, 2021.

The downloadable file is a poster presentation with audio commentary with a run time of 5:46.


Available to Ursinus community only.