Skip to main content

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

Buy Article:

$63.00 plus tax (Refund Policy)

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.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

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

Document Type: Review Article

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

Publication date: 01 October 2003

More about this publication?
  • 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.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more