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2000
Volume 10, Issue 5
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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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/content/journals/ppl/10.2174/0929866033478672
2003-10-01
2025-05-22
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