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Updated: Jul 7, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
A solid-state 17O NMR study of L -phenylalanine and L -valine hydrochlorides
Kazuhiko Yamada1, Tadashi Shimizu, Shinobu Ohki
1National Institute for Materials Science, 3-13 Sakura, Tsukuba, Ibaraki 305-0003, Japan. YAMADA.Kazuhiko@nims.go.jp
Abstract:
We have presented an experimental investigation of the oxygen-17 chemical shielding (CS) and electric-field-gradient (EFG) tensors for alpha-COOH groups in polycrystalline amino acid hydrochlorides. The 17O CS and EFG tensors including the relative orientations between the two NMR tensors are determined in [17O]-L-phenylalanine hydrochloride and [17O]-L-valine hydrochloride by the analysis of the 17O magic-angle-spinning (MAS) and stationary NMR spectra obtained at 9.4, 11.7, 16.4, and 21.8 T. The quadrupole coupling constants (CQ) and the span of the CS tensors are found to be 8.41-8.55 MHz and 7.35-7.41MHz, and 548-570 ppm and 225-231 ppm, for carbonyl and hydroxyl oxygen atoms, respectively. Extensive quantum chemical calculations using density functional theory (DFT) have been also carried out for a hydrogen-bonding model. It is demonstrated that the behavior of the dependence of hydrogen-bond distances on 17O NMR tensors for the halogen ions is different from those for the water molecule.
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