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Abstract

Heat shock proteins (HSPs) are a highly conserved family of proteins critical to both environmental stress response and cellular function under normal conditions. More specifically HSPs are chaperone proteins that work to refold other misfolded proteins. Data suggests that HSPs have neuroprotective effects against protein aggregation diseases such as Alzheimer's. Previous research indicates that HSP70 has evolved multiple isoforms or variants in organisms such as the sea anemone Nematostella vectensis and Saccharomyces cerevisiae budding yeast. While the presence of these isoforms is established, the function and evolutionary history is not fully understood. The purpose of this research is to contribute towards a better understanding of the HSP70 isoforms. Presented at the 2022 UNC Charlotte Undergraduate Research Conference.

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