Class Year

2014

Date

4-17-2014

Document Type

Thesis

Distinguished Thesis

Yes

Degree Name

Bachelor of Arts (BA)

Department or Program

Biology

First Advisor

Shubhik DebBurman

Second Advisor

Ann B. Maine

Third Advisor

Matthew R. Kelley

Abstract

Parkinson’s disease (PD) is a disease in which neurons in the substantia nigra die. Within these neurons are Lewy bodies, proteinatious aggregates composed primarily of α-synuclein. Two important questions in PD research are these: are some amino acids more important in the properties of α-synuclein; how ar e naturally-occurring C-terminal truncations to α-synuclein relevant to pathology? My senior thesis explores both questions. To evaluate the importance of specific amino acids, I made point mutations on implicated amino acids: D2, A76, V77, Q79, and E83. I hypothesized that these mutations would either diminish or enhance the pathological properties of α-synuclein. I found that these amino acids are important for t h e properties o f α-synuclein. To study the relevance of truncations, I recreated four naturally occurring truncations. I hypothesized that t h e truncations would result in aggregations because of the solubility properties of the C-terminus. Truncation resulted in less membrane binding and cytoplasmic punctate foci.

Available for download on Monday, May 01, 2034


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