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We wanted to explore the effects of changing the amino acid Isoleucine to Leucine, Valine and Alanine on the folding/unfolding rate of the protein FynSH3. This was done by genetic re-engineering of the protein to include the amino acids of our choice. We then characterized the folding/unfolding rates using a stop-flow apparatus and found that although the stability varied if that factor was accounted for the rate of folding was found not to vary. Previous work had stated that the replacement of Isoleucine with Alanine produced a significant difference. Our work refuted this claim and indicated it was more a stability difference.
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| Attachment | Size |
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 Download Research Presentation as a PDF file | 303.3 KB |
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My research was in the area of protein folding, trying to understand the mechanism of how a simple 50 amino acid residue protein chain goes from its unfolded to its folded state. Alzheimer’s disease is the result of misfolded proteins. These proteins then form plaques (piles of junk) in the brain and reduce or stop brain function ( i.e. you can’t remember your name). My project combines at a very basic level the study of organic chemistry with the underlying theme of trying to understand proteins and how they fold. This gives much more relevance to what appears at first to be a very esoteric form of chemistry.y.
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| Attachment | Size |
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 Download Curriculum Project | 150.5 KB |