Document Type
Paper- Restricted to Campus Access
Publication Date
4-29-2026
Faculty Mentor
Samantha Wilner
Abstract
In Biochemistry II lab, we are using the Biochemistry Authentic Scientific Inquiry Lab (BASIL) model to test our protein of interest. The BASIL lab aims to define the function of a protein with known structure. The protein data bank (PDB) identifies our protein on interest as 4DIU. Through both wet lab and in silico techniques including purification, amplification, and analysis, we have predicted that our protein is an ester or lipid hydrolase of the alpha/beta hydrolase superfamily. 4DIU was expressed in E. coli BL21De3 cells and then purified using nickel affinity chromatography. SDS-PAGE analysis confirmed that we purified a protein between 25-30 kDa, which is the predicted molecular weight of 4DIU. As a hydrolase, we have determined that our protein is able to use water molecules within compounds, such as esters or lipids, in order to break them apart.
Recommended Citation
Nevison, Alexandria Kay and Brown, Abby, "Breaking Bonds: A Study of the Hydrolase of 4DIU" (2026). Biochemistry and Molecular Biology Presentations. 28.
https://digitalcommons.ursinus.edu/biochem_pres/28
Restricted
Available to Ursinus community only.
Comments
Presented as part of the Ursinus College Celebration of Student Achievement (CoSA) held April 29, 2026.
The downloadable file is a PowerPoint poster.