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.