Mapping intramolecular distances of the 18.5-kDa Myelin Basic Protein under various conditions by Förster Resonance Energy Transfer

dc.contributor.advisorGeorge, Harauz
dc.contributor.authorAnonna, Prioti
dc.date.accessioned2019-12-20T20:45:03Z
dc.date.available2019-12-20T20:45:03Z
dc.date.copyright2019-12-13
dc.date.created2019-12-13
dc.date.issued2019-12-20
dc.degree.departmentDepartment of Molecular and Cellular Biologyen_US
dc.degree.grantorUniversity of Guelphen_US
dc.degree.nameMaster of Scienceen_US
dc.degree.programmeMolecular and Cellular Biologyen_US
dc.description.abstractThe predominant 18.5-kDa isoform of Myelin Basic Protein (MBP) is essential for the development of myelin in the central nervous system (CNS), and is hyper-deiminated in multiple sclerosis. We have previously obtained intramolecular distances between several single Cys-substituted sites in unmodified and pseudo-deiminated MBP variants, and a single internal Trp residue, by Förster Resonance Energy Transfer (FRET). I have obtained additional constraints by FRET of fluorophores attached to double- and single-Cys-substituted residues in the presence of dodecylphosphocholine (DPC) and Zn2+ (to mimic the myelin membrane per se). The quenching of Trp fluorescence by the acceptor showed that Zn2+ in the presence of DPC at its critical micelle concentration of 1.25 mM affected MBP’s local tertiary fold, but FRET distances indicated a negligible effect on global structure. We showed that DPC, like trifluoroethanol (TFE), caused slight compaction and extension. No significant differences between the two variants were seen.en_US
dc.description.sponsorshipNatural Sciences and Engineering Research Council of Canada
dc.identifier.urihttp://hdl.handle.net/10214/17690
dc.language.isoenen_US
dc.publisherUniversity of Guelphen_US
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectmultiple sclerosisen_US
dc.subjectmyelin basic proteinen_US
dc.subjectFRETen_US
dc.titleMapping intramolecular distances of the 18.5-kDa Myelin Basic Protein under various conditions by Förster Resonance Energy Transferen_US
dc.typeThesisen_US

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