Researcher ORCID Identifier
0000-0001-6043-372X
Graduation Year
2022
Document Type
Open Access Senior Thesis
Degree Name
Bachelor of Arts
Department
Chemistry
Reader 1
Bethany Caulkins
Reader 2
Mary Hatcher-Skeers
Terms of Use & License Information
Rights Information
@2021 Julia R Didziulis
Abstract
Ubiquitination and other post-translational modifications play a major role in the proliferation of many neurodegenerative diseases, developmental disorders, and cancers, and as such are subjects of recently increased biochemical interest. Expanding upon such research, this study confirmed a robust method of ubiquitin expression and purification, then used 15N-1H HSQC to analyze ubiquitin samples containing varying concentrations of a deep cavitand with affinity for lysine and arginine side chains. In the pure ubiquitin spectrum, arginine side chain chemical shifts were detected in the nitrogen 80-85 ppm range and lysine side chain signals were undetected. However, upon introduction of the cavitand, collection of chemical shift perturbation data was prohibited by the cavitand precipitating out of solution. To overcome this obstacle, future experiments may benefit by refining the purification protocol via size-exclusion chromatography or adjusting sample properties such as pH, salt content, and more. Once complete, these experiments may indicate the cavitand’s viability as a biosensor for ubiquitination and other modifications, possibly accelerating diagnostics and disease research as a result.
Recommended Citation
Didziulis, Julia, "Here, There, and Everywhere: Probing Ubiquitin-Cavitand Binding via 15N-1H HSQC" (2022). Scripps Senior Theses. 1928.
https://scholarship.claremont.edu/scripps_theses/1928
