Graduation Year


Date of Submission


Document Type

Campus Only Senior Thesis

Degree Name

Bachelor of Arts



Reader 1

Bethany Caulkins

Reader 2

Joel Mackey


Ubiquitin holds vast biological consequences by functioning as a post translational modification signaling for degradation and regulation at the cellular level. Signaling is dependent on how a substrate is ubiquitylated since different sites lead to different outcomes. Cavitand is a synthetic self-folding molecule that acts as a biosensor for modified residues. To understand if cavitand can function as a biosensor for ubiquitinated substrates, the binding site between ubiquitin and cavitand must first be understood. This study aims to investigate the ubiquitin-cavitand binding pocket through 1H-15N HSQC NMR. To begin, human ubiquitin was expressed and purified. However, an obstacle was reached in the purification process since the protein was not properly binding to the resin. Modified purification protocols were carried out to try and find the issue. Since a successful modification was found, we can now move forward with the experiment to observe the binding interactions of ubiquitin cavitand.

This thesis is restricted to the Claremont Colleges current faculty, students, and staff.