Extracellular domain of myelin oligodendrocyte glycoprotein (MOG) exhibits solvent-dependent conformational transitions.
- 1 October 2003
- journal article
- Published by Bentham Science Publishers Ltd. in Protein & Peptide Letters
- Vol. 10 (5) , 483-490
- https://doi.org/10.2174/0929866033478672
Abstract
Abstract: The conformation of the non-glycosylated recombinant form of the extracellar domain of rat MOG (rMOG(1-125)) dissolved in different solvent conditions was studied by CD spectroscopy. The results show that rMOG(1-125) exhibits a predominantly β sheet conformation in aqueous buffer solution at pH 7.5 and that this β-form is stabilized by zwitterionic phospholipids, DPC and LPCP. The a helical content of the protein can increase from 9% to up to 20% when TFE or anionic detergent LPAP and SDS are added.Keywords
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