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Date of Award


Document Type

Restricted Thesis: Campus only access

Degree Name

Bachelor of Science


Biochemistry & Molecular Biol.

First Advisor

Dr. John M. Warrick


Polyglutamine diseases are dominantly inherited, neurodegenerative diseases caused by an expansion of a glutamine repeat within the protein coding region of the gene (1). The severity of these diseases depends on the length of the expanded region of glutamines within the protein, with a certain threshold leading to neuronal loss and a degenerative phenotype (2-4). Typically, a longer repeat leads to more severe disease toxicity and an earlier onset, although the minimum number of repeats leading to a degenerative phenotype varies by disease (2-5). Besides sharing this dynamic and unstable expanded CAG repeat and causing neurodegeneration, the polyglutamine diseases have very little in common. The host proteins for the polyglutamine tract are unrelated in each disease (2-4), and based on the protein’s subcellular localization, structure, activity, and biological role, the expansion affects the proteins uniquely (4,6).