Characterization of 15N chemical shift tensors via 15N-13C REDOR and 1N-1H dipolar-shift CPMAS NMR spectroscopy.
As part of our studies on the characterization of 15N chemical shift anisotropy (CSA) via magic angle spinning (MAS) NMR spectroscopy, we have investigated via numerical simulations the sensitivity of two different REDOR experimental protocols to the angles defining the orientation of the 15N-13C' bond vector in the principal axis system of the 15N CSA tensor of the amide nitrogen in a peptide bond. Additionally, employing polycrystalline samples of 15N and 13C', 15N-labeled acetanilide, we have obtained, in a first study of this type, the orientation of the 15N CSA tensor in the molecular frame by orienting the tensor with respect to the 15N-3C' and 15N-1H dipolar vectors via 15N-13C' REDOR and 15N-1H dipolar-shift MAS experiments, respectively.
Heise
B
B
Abteilung Molekulare Biophysik/NMR Spektroskopie, Institut für Molekulare Biotechnologie, Jena, Germany.
Leppert
J
J
Ramachandran
R
R
D000083:Acetanilides / Q000737:chemistry*; D000577:Amides / Q000737:chemistry; D016880:Anisotropy; D002247:Carbon Isotopes; D003198:Computer Simulation; D003460:Crystallization; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008432:Mathematical Computing; D009587:Nitrogen Isotopes; D010455:Peptides / Q000737:chemistry; D011522:Protons
D000083:Acetanilides; D000577:Amides; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010455:Peptides; D011522:Protons