High-speed magic angle spinning solid-state 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers.
One- and two-dimensional solid-state 1H nuclear magnetic resonance spectra of gramicidin A incorporated in a dimyristoylphosphatidylcholine membrane have been obtained with use of high-speed magic angle spinning. By rotating the sample at 13 kHz, it is possible to observe signals in the 1H spectra between 6.0 and 9.0 ppm attributable to the aromatic protons of the tryptophan residues and the formyl group proton of gramicidin A. Two-dimensional solid-state COSY spectra provided information for the peak assignments. Moreover, changes in the 1H spectra have been observed as a function of the co-solubilization solvent initially used to prepare the samples and therefore as a function of the conformation adopted by gramicidin A. Three organic solvents have been used: trifluoroethanol, a mixture of methanol/chloroform (1:1 v/v), and ethanol. The conformational interconversion of gramicidin A from the double helix conformation to the channel structure for the sample prepared from ethanol was confirmed by following the time evolution of the proton spectra.
Bouchard
M
M
Département de Chimie, Université Laval, Québec, Canada.
Davis
J H
JH
Auger
M
M
D055592:Biophysical Phenomena; D001703:Biophysics; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D006096:Gramicidin / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry; D007700:Kinetics; D008051:Lipid Bilayers / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012997:Solvents; D014364:Tryptophan / Q000737:chemistry
D008051:Lipid Bilayers; D012997:Solvents; D006096:Gramicidin; D006859:Hydrogen; D014364:Tryptophan; D004134:Dimyristoylphosphatidylcholine