Studies by Undergraduate Researchers at Guelph (SURG) Biophysical characterization of 21.5-kDa myelin basic protein (MBP) and the effects of zinc on its structure

Danielle Lanthier, Kenrick Vassall, George Harauz
unpublished
Myelin Basic Protein (MBP) is a highly abundant protein in central nervous system (CNS) myelin that has a critical role in its proper formation and functioning. The 21.5-kDa isoform of MBP has been shown to be selectively imported into the nucleus of myelin-producing cells, oligodendrocytes, and may be involved in signaling pathways that affect the formation and recovery of CNS myelin. The first step in understanding potential nuclear binding partners of 21.5-kDa MBP is to characterize the
more » ... ture of the protein. In this study, circular dichroism and fluorescence spectroscopy were used to analyze the structure of 21.5-kDa rmMBP (recombinant murine MBP) in vitro in the presence and absence of Zn 2+ , an abundant trace metal in CNS myelin that has been suggested to affect MBP structure. Fluorescence spectroscopy with a probe for hydrophobic protein regions showed that Zn 2+ may affect the conformation of 21.5-kDa MBP in aqueous solution.
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