HIGH-RESOLUTION CONFORMATION OF GRAMICIDIN-A IN A LIPID BILAYER BY SOLID-STATE NMR

被引：622
作者：
KETCHEM, RR
HU, W
CROSS, TA
机构：
[1] FLORIDA STATE UNIV,INST MOLEC BIOPHYS,NATL HIGH MAGNET FIELD LAB,TALLAHASSEE,FL 32306
[2] FLORIDA STATE UNIV,DEPT CHEM,TALLAHASSEE,FL 32306
来源：
SCIENCE | 1993年 / 261卷 / 5127期
关键词：
D O I：
10.1126/science.7690158
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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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页码：1457 / 1460
页数：4
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