Abstract
Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic gradient across certain cell membranes. Two-dimensional 1H NMR spectroscopy was used to investigate the structure of the peptide in three of the membrane environments most commonly employed in biophysical studies. Sequence-specific resonance assignments were determined for the peptide in perdeuterated dodecylphosphocholine (DPC) and sodium dodecylsulfate micelles and confirmed for the peptide in 2,2,2-trifluoroethanol solution. The secondary structure is shown to be helical in all of the solvent systems. The NMR data were used as a set of restraints for a simulated annealing protocol that generated a family of three-dimensional structures of the peptide in DPC micelles, which superimposed best between residues 4 and 20. For these residues, the mean pairwise rms difference for the backbone atoms is 0.47 +/- 0.10 A from the average structure. The calculated peptide structures appear to be curved, with the bend centered at residues Phe12 and Gly13.
- acid
- agents,antimicrobial
- amino
- cationic
- data,peptides,phosphorylcholine,protein
- dodecyl
- peptides,deuterium,hydrogen,magainins,magnetic
- proteins
- resonance
- sequence
- sequence,anti-infective
- spectroscopy,micelles,models,molecular,molecular
- structure,secondary,sodium
- sulfate,solutions,trifluoroethanol,water,xenopus
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