High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR

Science. 1993 Sep 10;261(5127):1457-60. doi: 10.1126/science.7690158.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Gramicidin / chemistry*
  • Hydrogen Bonding
  • Lipid Bilayers / chemistry*
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Protein Structure, Secondary


  • Lipid Bilayers
  • Gramicidin