Submission Date

7-19-2024

Document Type

Paper- Restricted to Campus Access

Department

Biology

Faculty Mentor

Dale Cameron

Second Faculty Mentor

Christina Kelly

Comments

Presented during the 26th Annual Summer Fellows Symposium, July 19, 2024 at Ursinus College.

This research was funded by a grant from the National Institutes of Health.

Project Description

Proteins are large biological macromolecules that are made up of chains of smaller building blocks called amino acids. They serve many important functions in cells. For example, proteins include enzymes, storage proteins, receptor proteins, antibodies, and many others. Chaperone proteins help the amino acid chains that form these proteins to fold into the correct structures. Without chaperone proteins, amino acid chains can misfold into incorrect structures and form prions. Prions can interact with correctly folded copies of the same protein and cause them to misfold and bind together, thus causing a protein aggregate. My project sought to determine the interaction between the RAC and NAC subunits, two chaperone proteins, by engineering yeast strains with deletions of components of RAC, NAC, or both. By measuring prion formation in the strains I have engineered, we will be able to understand how the presence of both the RAC and the NAC help prevent the formation of prions within cells.

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