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
Protein & Peptide Letters
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.
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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
DOI https://dx.doi.org/10.2174/0929866033478672 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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