1H-NMR study of gramicidin A transmembrane ion channel. Head-to-head right-handed, single-stranded helices

FEBS Letters

Volumn 186, Issue 2, 1985, Pages 168-174

  Arseniev, A S ^a   Barsukov, I L ^a   Bystrov, V F ^a   Lomize, A L ^a   Ovchinnikov, Yu A ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Gramicidin A; Ion channel; NMR; Nuclear Overhauser effect; Peptide conformation; Single stranded helix

Indexed keywords

GRAMICIDIN A; ION CHANNEL; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DODECYL SULFATE SODIUM; GRAMICIDIN;

NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; ARTICLE; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; ION CHANNEL; METABOLISM; MICELLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION;

CIRCULAR DICHROISM; DIMYRISTOYLPHOSPHATIDYLCHOLINE; GRAMICIDIN; ION CHANNELS; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; SODIUM DODECYL SULFATE;

EID: 0021892874     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(85)80702-X     Document Type: Article

References (26)

1. Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids
2. Conformational dependence of the vicinal proton coupling constant for the CαCβ bond in peptides