Structure of an isolated gramicidin A double helical species by high-resolution nuclear magnetic resonance
- 20 August 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 226 (4), 1101-1109
- https://doi.org/10.1016/0022-2836(92)91055-t
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Solvent history dependence of gramicidin A conformations in hydrated lipid bilayersBiophysical Journal, 1988
- Three-Dimensional Structure at 0.86 Å of the Uncomplexed form of the Transmembrane Ion Channel Peptide Gramicidin AScience, 1988
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- NMR solution structure of gramicidin A complex with caesium cationsFEBS Letters, 1985
- Gramicidin ChannelsAnnual Review of Physiology, 1984
- NMR solution conformation of gramicidin A double helixFEBS Letters, 1984
- Hydrogen bonding in globular proteinsProgress in Biophysics and Molecular Biology, 1984
- 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
- Investigation of exchange processes by two-dimensional NMR spectroscopyThe Journal of Chemical Physics, 1979
- The peptide antibiotics of Bacillus: chemistry, biogenesis, and possible functionsMicrobiology and Molecular Biology Reviews, 1977