Extracellular Domain Of Myelin Oligodendrocyte Glycoprotein (Mog) Exhibits Solvent-Dependent Conformational Transitions

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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: Myelin Oligodendrocyte Glycoprotein (Mog); non-glycosylated; zwitterionic phospholipids

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866033478672

Affiliations: Department of Chemistry, University of South Alabama, Mobile, AL 36688, USA

Publication date: October 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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