Document Type

Paper- Restricted to Campus Access

Publication Date


Faculty Mentor

Dale Cameron


In order to be useful, our genetic information needs to be translated into functional proteins. Proteins carry out many important functions within our cells. Once built, proteins must fold in specific and correct ways to function properly. When proteins misfold they can be very detrimental to the organism, since misfolded proteins can lose their intended function or potentially even acquire new, harmful functions. One classification of misfolded proteins is called prions. Prions are able to interact with correctly folded copies of the same type of proteins and transform them into the misfolded prion structure. These misfolded proteins can then clump together to form aggregates that are associated with mammalian neurological diseases. However, while in mammals, prions cause diseases, it has been shown that in yeast, prions may provide a fitness advantage in some environments. Previous work from our lab has shown that cells with the [PSI+] prion have reduced levels of glucose transporters. Therefore, to begin to investigate possible biological consequences of [PSI+] prion formation, I measured glucose uptake under various conditions to observe any differences that may be attributable to the presence of prions.


Presented as part of the Ursinus College Celebration of Student Achievement (CoSA) held April 23 – April 30, 2020.

The downloadable file is an MP4 video with recorded audio commentary.


Available to Ursinus community only.