Abstract
The magnitudes and orientations of the principal elements of the 15N chemical shift and 1H−15N dipolar coupling interaction tensors pertaining to the glycine residue in 15N-acetyl glycine (NAG) and [15N-Gly]collagen were determined by the analysis of one-dimensional dipolar chemical shift powder patterns. A one-dimensional 1H−15N dipolar 15N chemical shift spectrum was obtained on a [15N-Gly]collagen fiber sample with the fiber axis oriented parallel to the external magnetic field. The dipolar chemical shift spectrum enabled the orientation of the peptide plane to be determined relative to the direction of the applied magnetic field or the triple-helix axis of the collagen fiber. The magnitudes of the principal elements of the tensors and their orientations in the molecular frame for these two sites are quite different. The magnitudes of the chemical shift tensors are 42.3, 67, and 223.4 ppm for [15N-Gly]collagen and 37, 82.8, and 220.4 ppm for NAG. The angle (βN) between the least shielded 15N chemical s...
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