A Computational Study of Amyloid Fibrils and their Structural Properties

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dc.contributor.advisorHansmann, Ulrich
dc.contributor.authorAlred, Erik
dc.contributor.committeeMemberBarnes, Ronald
dc.contributor.committeeMemberMao, Chuanbin
dc.contributor.committeeMemberSchroeder, Susan
dc.contributor.committeeMemberRajan, Rakhi
dc.date.accessioned2017-10-19T17:15:02Z
dc.date.available2017-10-19T17:15:02Z
dc.date.issued2017-12
dc.date.manuscript2017-08-23
dc.description.abstractThe term amyloid describes misfolded protein aggregates in which a highly ordered cross β-sheet pattern is adopted. While there exist functional amyloids, the majority of known amyloids are associated with diseases in multicellular organisms. One example is the association is that between Amyloid β (Aβ) and Alzheimer’s disease, a neurodegenerative disorder in humans. Several mechanisms of toxicity have been proposed, yet a lack of dynamic data prevents a full molecular explanation for the toxicity of Aβ and other amyloid systems. Mutational effects often increase the degree of polymorphism in observable structures, compounding the issues with a molecular level examination. In this thesis, Molecular Dynamic (MD) simulations of wild-type and mutant sequences of both Aβ and Prion proteins are performed to explore the structural dynamics of amyloids and amyloid-like systems. The data generated will provide physics-based explanations of the traits of amyloids on a molecular level which may guide further physical experimentation into the mechanism of amyloid toxicity and formation.en_US
dc.identifier.urihttp://hdl.handle.net/11244/52386
dc.languageen_USen_US
dc.subjectAmyloiden_US
dc.subjectProtein Aggreagationen_US
dc.subjectStructural Biochemistryen_US
dc.subjectPrionen_US
dc.subjectChemistry, Biochemistry.en_US
dc.thesis.degreePh.D.en_US
dc.titleA Computational Study of Amyloid Fibrils and their Structural Propertiesen_US
ou.groupCollege of Arts and Sciences::Department of Chemistry and Biochemistryen_US
shareok.orcid0000-0002-1414-0894en_US

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