Determination of the structure of a membrane-incorporated ion channel. Solid-state nuclear magnetic resonance studies of gramicidin A
- 1 August 1989
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 56 (2) , 307-314
- https://doi.org/10.1016/s0006-3495(89)82677-3
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Structural fluctuations of a helical polypeptide traversing a lipid bilayer.Proceedings of the National Academy of Sciences, 1988
- The structure of melittinEuropean Journal of Biochemistry, 1988
- Solid-phase peptide synthesis and solid-state NMR spectroscopy of [Ala3-15N][Val1]gramicidin A.Proceedings of the National Academy of Sciences, 1988
- Deuterium nuclear magnetic resonances of exchange-labeled gramicidin in an oriented lyotropic nematic phaseBiochemistry, 1988
- Structure and dynamics of the Pf1 filamentous bacteriophage coat protein in micellesBiochemistry, 1987
- NMR structural analysis of a membrane protein: bacteriorhodopsin peptide backbone orientation and motionBiochemistry, 1985
- Dynamic properties of the backbone of an integral membrane polypeptide measured by 2H-NMREuropean Biophysics Journal, 1985
- Is the Gramicidin A Transmembrane Channel Single-Stranded or Double-Stranded Helix? A Simple Unequivocal DeterminationScience, 1983
- Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reactionAnalytical Biochemistry, 1981
- First observation of amino acid side chain dynamics in membrane proteins using high field deuterium nuclear magnetic resonance spectroscopy.Journal of Biological Chemistry, 1981