Extracellular Domain Of Myelin Oligodendrocyte Glycoprotein (Mog) Exhibits Solvent-Dependent Conformational Transitions
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.
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Document Type: Review Article
Affiliations: Department of Chemistry, University of South Alabama, Mobile, AL 36688, USA
Publication date: 01 October 2003
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