Structural and functional studies of ion channels
by solid-state 17O NMR spectroscopy:
gramicidin A
E.Chekmenev,  J.Hu,  Z.Gan,  P.Gor'kov,  W.Brey  (NHMFL)

Static ¹⁷O ¹H decoupled spectrum of ¹⁷O-Leu10-gramicidin A in oriented DMPC lipid bilayers acquired at 900 MHz. 5 mg of peptide of 57% ¹⁷O enriched, 1:16 peptide-to-lipid molar ratio, 70k transients at 40°C. Parallel and perpendicular orientations of the ion channel with respect to magnetic field correspond to the top and bottom spectra respectively. The peaks 0-100 ppm correspond to the background signal of lipids and water.

***

17O solid-state NMR study of carbonyl sites in peptides
E.Chekmenev,  Z.Gan (NHMFL),  R.Wittebort (UofL)

1H decoupled ¹⁷O static (left) and MAS (right) spectra (blue) and simulations (red) of Ala-(Gly-¹⁷O)-Gly (top row) and Gly-(Gly-¹⁷O)-Val (bottom row). Static spectra of glycyl carbonyl oxygens were acquired at 21.2 T while 12.5 kHz MAS spectra were obtained at 14.1 T. All spectra are referred to external liquid water and were simulated with home-written MATLAB program.

... back to 900 page