ISSN:
1573-5001
Keywords:
Channel structure
;
Magainin
;
Acetylcholine receptor
;
Lipid bilayer
;
Amphiphilic α-helix
;
15N chemical shift
;
Solid-state NMR
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary Solid-state NMR spectroscopy was used to determine the orientations of two amphipathic helical peptides associated with lipid bilayers. A single spectral parameter provides sufficient orientational information for these peptides, which are known, from other methods, to be helical. The orientations of the peptides were determined using the15N chemical shift observed for specifically labeled peptide sites. Magainin, an antibiotic peptide from frog skin, was found to lie in the plane of the bilayer. M2δ, a helical segment of the nicotinic acetylcholine receptor, was found to span the membrane, perpendicular to the plane of the bilayer. These findings have important implications for the mechanisms of biological functions of these peptides.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01877228
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