Protein misfolding and aggregation has been linked to neurodegenerative diseases, such as Alzheimer’s and Huntington’s disease. Successful protein folding is a consequence of molecular chaperones, which are proteins that are responsible for leading and guiding other proteins to fold successfully to their native state. Similarly, it has been indicated that nucleic acids, such as RNA and DNA, can also aid protein folding, and thus prevent protein aggregation by acting as strong molecular chaperones. This research project seeks to analyze how nucleic acids can affect the folding of TagRFP675, a red fluorescent protein, in vitro.

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