Journal
AMINO ACIDS
Volume 42, Issue 4, Pages 1467-1474Publisher
SPRINGER
DOI: 10.1007/s00726-011-0911-5
Keywords
Myelin; Peptide; Synchrotron radiation; Folding; Micelle
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Funding
- Academy of Finland
- Sigrid Juselius Foundation
- Magnus Ehrnrooth Foundation
- Department of Biochemistry, University of Oulu
- European Community [BESSY-09.1.80843, FP7/2007-2013, 226716]
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Myelin is a tightly packed membrane multilayer in the nervous system, which harbours a specific set of quantitatively major proteins. All these proteins interact with the lipid bilayer, being either peripheral or integral membrane proteins. In this study, we examined the conformational properties of peptides from the myelin proteins P0, CNPase, MOBP, P2 and MOG, using trifluoroethanol and micelles of different detergents as membrane-like mimics. The peptides showed significant differences in their folding under the employed conditions, as evidenced by synchrotron radiation circular dichroism spectroscopy. Our experiments provide new structural information on the interactions between myelin proteins and membranes, using a simplified model system of synthetic peptides and micelles.
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