Analysis of Alpha Helices in the Receptor Binding Domain in Botulinum Types A, B, D, G

dc.contributor.advisor	Griffin, Jediddiah
dc.creator	Topp, Dakota
dc.date.accessioned	2021-04-13T19:09:54Z
dc.date.available	2021-04-13T19:09:54Z
dc.date.issued	2021
dc.description.abstract	Botulinum toxin is a protein secreted by the bacteria Clostridium Botulinum and has seven types denoted A-G. Human botulism is only caused by types A and B, the other five species are nontoxic to humans. This research used a series of computational programs to analyze types A, B, D and G. The receptor binding domain was analyzed, primarily the main alpha helix of the active site. It was found that this alpha helix had varying polarity and charge consistent with the toxicity, a more polar positive chain was found in types A and B in comparison with a negative charge associated with types D and G. In addition, a computational analysis of the overall structure was completed, however it was found there were minimal differences in structure despite varying amino acid compositions. An inference can be made that the differences in amino acid composition, causing variances in the polarity and charge is a causative agent in the toxicity of different types of botulinum toxin.	en_US
dc.identifier.uri	http://hdl.handle.net/11558/5826
dc.language.iso	en_US	en_US
dc.subject	Botulinium Toxin	en_US
dc.subject	Alpha Helix	en_US
dc.subject	Polarity	en_US
dc.subject	RISE Above Research Conference	en_US
dc.title	Analysis of Alpha Helices in the Receptor Binding Domain in Botulinum Types A, B, D, G	en_US
dc.type	Other	en_US

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