High-Resolution Conformation of Gramicidin A in a Lipid Bilayer by Solid-State NMR
- 10 September 1993
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 261 (5127), 1457-1460
- https://doi.org/10.1126/science.7690158
Abstract
Solid-state nuclear magnetic resonance spectroscopy of uniformly aligned preparations of gramicidin A in lipid bilayers has been used to elucidate a high-resolution dimeric structure of the cation channel conformation solely on the basis of the amino acid sequence and 144 orientational constraints. This initial structure defines the helical pitch as single-stranded, fixes the number of residues per turn at six to seven, specifies the helix sense as right-handed, and identifies the hydrogen bonds. Refinement of this initial structure yields reasonable hydrogen-bonding distances with only minimal changes in the torsion angles.Keywords
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