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- W2898496741 abstract "Abstract The acquisition of 14 N NMR spectra in solid samples is challenging due to quadrupolar couplings with magnitudes up to several MHz. This nucleus is nonetheless important as it is involved in the formation of essential secondary structures in biological systems. Here we report the structural study of the atomic environment of amide functions in polypeptides using magic-angle spinning NMR spectroscopy of the ubiquitous 14 N isotope. The cyclic undecapeptide cyclosporin, in which only four hydrogen atoms are directly bound to nitrogen atoms, is chosen for illustration. Structural details of different environments can be revealed without resorting to isotopic enrichment. The network of inter- and intra-residue dipolar couplings between amide 14 N nuclei and nearby protons can be probed and mapped out up to a tunable cutoff distance. Density functional theory calculations of NMR quadrupolar interaction tensors agree well with the experimental evidence and allow the unambiguous assignment of all four non-methylated NH nitrogen sites and neighboring proton nuclei." @default.
- W2898496741 created "2018-11-02" @default.
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- W2898496741 date "2018-11-01" @default.
- W2898496741 modified "2023-10-06" @default.
- W2898496741 title "Dipolar couplings in solid polypeptides probed by 14N NMR spectroscopy" @default.
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- W2898496741 doi "https://doi.org/10.1038/s42004-018-0072-5" @default.
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