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The 18.5-kDa Myelin Basic Protein has Loose Tertiary Contacts Regulated by Zinc and Post-Translational Modification

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dc.contributor.advisor Harauz, George
dc.contributor.author Fayaz, Ehsan
dc.date.accessioned 2011-12-20T16:16:32Z
dc.date.available 2012-11-27T06:00:12Z
dc.date.copyright 2011-12
dc.date.created 2011-11-16
dc.date.issued 2011-12-20
dc.identifier.uri http://hdl.handle.net/10214/3202
dc.description.abstract Myelin basic protein (MBP) has fascinated researchers and clinicians alike due to its major structural role in myelin and the central nervous system, and its potent auto-immunogenic properties that cause demyelination in animal models. The charge variants of MBP have been of particular interest. The C1 component, the least modified and most cationic of the variants, is the most abundant form of MBP in healthy adult myelin. The C8 component, the most modified and the least cationic variant, has been found in higher proportions in myelin of MS patients and children. Here, an investigation of the structural differences between C1 and C8 components of MBP was conducted. The spectral and hydrodynamic properties of these variants were monitored via a number of biophysical/biochemical techniques. The effect of zinc (Zn2+) on the conformational behaviour of MBP was examined. Zn2+ is an abundant metal in the brain, and had been previously shown to induce hydrodynamic compaction in MBP. Both variants have a loose tertiary arrangement with subtle differences. This arrangement is deficient in secondary structure and undergoes non-cooperative temperature-induced melting. Zn2+ stabilizes a molten globular-like state with enhanced ANS fluorescence, and promotes oligomerization. en_US
dc.language.iso en en_US
dc.subject Myelin en_US
dc.subject MBP en_US
dc.subject Protein en_US
dc.subject unstructured en_US
dc.subject fluorescence en_US
dc.subject saxs en_US
dc.subject oligomerization en_US
dc.subject demyelination en_US
dc.subject multiple sclerosis en_US
dc.subject disordered en_US
dc.subject zinc en_US
dc.subject divalent cations en_US
dc.subject structure en_US
dc.title The 18.5-kDa Myelin Basic Protein has Loose Tertiary Contacts Regulated by Zinc and Post-Translational Modification en_US
dc.type Thesis en_US
dc.degree.programme Biophysics en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Molecular and Cellular Biology en_US
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