%0 Journal Article %1 gesell_two-dimensional_1997 %A Gesell, J %A Zasloff, M %A Opella, S J %D 1997 %J J. Biomol. NMR %K 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 %N 2 %P 127--135 %T 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 %V 9 %X 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.

@article{gesell_two-dimensional_1997, 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.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Gesell, J and Zasloff, M and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2f0c15cf3d37155c88fb958e11c92c437/nmrresource}, interhash = {c148a4d4bb1aa4b877ce5089c01f8f8a}, intrahash = {f0c15cf3d37155c88fb958e11c92c437}, issn = {0925-2738}, journal = {J. Biomol. NMR}, keywords = {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}, month = feb, number = 2, pages = {127--135}, pmid = {9090128}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{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}}, volume = 9, year = 1997 }