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Science 10 September 1993:
Vol. 261. no. 5127, pp. 1457 - 1460
DOI: 10.1126/science.7690158
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Articles

Science, Vol 261, Issue 5127, 1457-1460
Copyright © 1993 by American Association for the Advancement of Science

articles

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

RR Ketchem, W Hu, and TA Cross

Institute of Molecular Biophysics, Florida State University, Tallahassee 32306.

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.


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Water: Foldase activity in catalyzing polypeptide conformational rearrangements.
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The conducting form of gramicidin A is a right-handed double-stranded double helix.
B. M. Burkhart, N. Li, D. A. Langs, W. A. Pangborn, and W. L. Duax (1998)
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Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers.
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