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

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

Volume: 10 Issue: 5

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

Affiliation:

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

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.

Cite this article as:

Ngu-Schwemlein Maria, Corzett Michele, Thornton H. Kevin, Balhorn Rod and Cosman Monique, Extracellular Domain Of Myelin Oligodendrocyte Glycoprotein (Mog) Exhibits Solvent-Dependent Conformational Transitions, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478672