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• W2006451625 abstract "The magnitudes and orientations of the principal elements of the 1H chemical shift, 1H−15N dipolar coupling, and 15N chemical shift interaction tensors in 15Nε1-tryptophan and 15Nπ-histidine nitrogen sites were determined by the analysis of three-dimensional powder patterns obtained from 15N-labeled powder samples of the amino acids. Although the magnitudes of the principal elements of the 1H and 15N chemical shift tensors for these two sites are quite different, their molecular orientations in the molecular frame are very similar. The least shielded 15N chemical shift tensor element, σ33N, and the most shielded 1H chemical shift tensor element, σ11H, are approximately colinear with the N−H bond in both cases. The principal elements, σ22H and σ22N, are in the plane of the indole ring for tryptophan and in the plane of the imidazole ring for histidine but oppose each other. σ11N and σ33H are perpendicular to the planes of these heterocyclic rings. The chemical shift tensors of the 1H and 15N nuclei in these two side chain nitrogen sites are distinctly different from those of backbone amide nitrogen sites." @default.
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• W2006451625 date "1997-10-01" @default.
• W2006451625 modified "2023-09-26" @default.
• W2006451625 title "Magnitudes and Orientations of the Principal Elements of the ¹H Chemical Shift, ¹H−¹⁵N Dipolar Coupling, and ¹⁵N Chemical Shift Interaction Tensors in ¹⁵N_ε1-Tryptophan and ¹⁵N_π-Histidine Side Chains Determined by Three-Dimensional Solid-State NMR Spectroscopy of Polycrystalline Samples" @default.
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• W2006451625 doi "https://doi.org/10.1021/ja9632670" @default.
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