Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
- 1 January 1997
- journal article
- research article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 9 (2) , 127-135
- https://doi.org/10.1023/a:1018698002314
Abstract
Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic gradient across certain cellmembranes. Two-dimensional 1H NMR spectroscopy was used to investigate the structure ofthe peptide in...Keywords
This publication has 51 references indexed in Scilit:
- Helix geometry in proteinsPublished by Elsevier ,2004
- Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopySolid State Nuclear Magnetic Resonance, 1996
- Conformation of a Peptide Corresponding to T4 Lysozyme Residues 59-81 by NMR and CD SpectroscopyBiochemistry, 1994
- Nicotinic Acetylcholine Receptor an 9 Å ResolutionJournal of Molecular Biology, 1993
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopyJournal of Biomolecular NMR, 1991
- Nuclear magnetic resonance investigation of the conformation of δ-haemolysin bound to dodecylphosphocholine micellesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filteringBiochemical and Biophysical Research Communications, 1983
- Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonanceJournal of Molecular Biology, 1983
- A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesBiochemical and Biophysical Research Communications, 1980