HIGH-RESOLUTION CONFORMATION OF GRAMICIDIN-A IN A LIPID BILAYER BY SOLID-STATE NMR
HIGH-RESOLUTION CONFORMATION OF GRAMICIDIN-A IN A LIPID BILAYER BY SOLID-STATE NMR
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DOI:
10.1126/science.7690158
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发表时间:
1993-09-10
期刊:
影响因子:
56.9
通讯作者:
CROSS, TA
中科院分区:
文献类型:
--
作者:
KETCHEM, RR;HU, W;CROSS, TA
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.