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dc.contributor.authorGiffin, James
dc.date.accessioned2016-05-11T16:08:16Z
dc.date.available2016-05-11T16:08:16Z
dc.date.issued2016-05-11T16:08:16Z
dc.identifier.urihttp://hdl.handle.net/10222/71675
dc.description.abstractProtein misfolding has increasingly been recognized to have causative roles in several human neurological diseases. Alpha-synuclein (αS) is a protein involved in the regulation of several neuronal synaptic functions. When misfolded and aggregated into an amyloid form, αS has been implicated in neuronal dysfunction and degeneration in Parkinson’s disease and related disorders. The goal of this project was to evaluate the effects of marine species-derived extracts from the Bay of Fundy, Canada, on the melting temperature of αS. Fractions that increased and decreased the α-synuclein melting temperature were identified within a single extract. These fractions were separated by acetone precipitation and size fractionation. The effects of fractions on amyloid formation were assessed. Compounds identified in this way may lead to novel marine-sourced products that directly prevent the protein misfolding that appears to be causative in Parkinson’s disease.en_US
dc.language.isoenen_US
dc.subjectalpha-synucleinen_US
dc.subjectparkinson's diseaseen_US
dc.subjectalgaeen_US
dc.subjectprotein foldingen_US
dc.subjectthermal shiften_US
dc.subjectamyloiden_US
dc.titleMODULATION OF ALPHA-SYNUCLEIN PROTEIN FOLDING BY A MARINE-SOURCED EXTRACTen_US
dc.date.defence2016-04-18
dc.contributor.departmentDepartment of Biologyen_US
dc.contributor.degreeMaster of Scienceen_US
dc.contributor.external-examinern/aen_US
dc.contributor.graduate-coordinatorSophia Stoneen_US
dc.contributor.thesis-readerTom MacRaeen_US
dc.contributor.thesis-readerNeil Rossen_US
dc.contributor.thesis-supervisorVanya Ewarten_US
dc.contributor.ethics-approvalNot Applicableen_US
dc.contributor.manuscriptsNot Applicableen_US
dc.contributor.copyright-releaseNot Applicableen_US
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