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. 1998 Feb;74(2 Pt 1):981–987. doi: 10.1016/S0006-3495(98)74021-4

Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy.

B Bechinger 1, M Zasloff 1, S J Opella 1
PMCID: PMC1302577  PMID: 9533709

Abstract

PGLa, a 21-residue member of the magainin family of antibiotic peptides, is shown to be helical between residues 6 and 21 when associated with detergent micelles by multidimensional solution nuclear magnetic resonance (NMR) spectroscopy. Solid-state NMR experiments on specifically 15N-labeled peptides in oriented phospholipid bilayer samples show that the helix axis is parallel to the plane of the bilayers. 15N solid-state NMR powder pattern line shapes obtained on unoriented samples demonstrate that the amino-terminal residues are highly mobile and that the fluctuations of backbone sites decrease from Ala6 toward the carboxy terminus. The powder pattern observed for 15N-labeled Ala20 is essentially that expected for a rigid site. These findings are similar to those for the 23-residue magainin2 peptide in membrane environments.

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Selected References

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