2mag
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NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES
OverviewOverview
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.
About this StructureAbout this Structure
2MAG is a Single protein structure of sequence from Xenopus laevis with NH2 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution., Gesell J, Zasloff M, Opella SJ, J Biomol NMR. 1997 Feb;9(2):127-35. PMID:9090128
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