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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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Title: The 18.5-kDa Myelin Basic Protein has Loose Tertiary Contacts Regulated by Zinc and Post-Translational Modification
Author: Fayaz, Ehsan
Department: Department of Molecular and Cellular Biology
Program: Biophysics
Advisor: Harauz, George
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.
URI: http://hdl.handle.net/10214/3202
Date: 2011-12-20


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