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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

Author(s): Maria Ngu-Schwemlein, Michele Corzett, Kevin H. Thornton, Rod Balhorn and Monique Cosman

Volume 10, Issue 5, 2003

Page: [483 - 490] Pages: 8

DOI: 10.2174/0929866033478672

Price: $65

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


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