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1 H‐NMR study of gramicidin A transmembrane ion channel
Author(s) -
Arseniev A.S.,
Barsukov I.L.,
Bystrov V.F.,
Lomize A.L.,
Ovchinnikov Yu.A.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80702-x
Subject(s) - gramicidin , chemistry , ion channel , transmembrane protein , ion , nuclear magnetic resonance , crystallography , physics , membrane , biochemistry , organic chemistry , receptor
The structure of[Val 1 ]gramicidin A incorporated into sodium dodecyl‐ d 25 sulphate micelles has been studied by two‐dimensional proton NMR spectroscopy. Analysis of nuclear Overhauser effects, spin‐spin couplings and solvent accessibility of NH groups show that the conformation of the Na + complex of gramicidin A in detergent micelles, which in many ways mimic the phospholipid bilayer of biomembranes, is an N‐terminal to N‐terminal (head‐to‐head) dimer formed by two right‐handed, single‐stranded β 6.3 helices with 6.3 residues per turn, differing from Urry's structure by handedness of the helices.