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Updated: Jan 14, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Triple-Resonance NMR Experiments for Assignment of Asparagine and Glutamine Side-Chain NH2 Groups in Intrinsically
Francesco Torricella1, G Marius Clore1, Vitali Tugarinov1
1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.
Abstract:
Complete degeneracy of aliphatic 13C chemical shifts of the same type of amino-acid residues precludes unambiguous NMR assignments of asparagine (Asn) and glutamine (Gln) carboxamide NH2 groups in intrinsically disordered proteins with conventional techniques. Here, a pair of triple-resonance NMR experiments is described that correlate the 1H/15N chemical shifts of Asn and Gln carboxamide NH2 groups with the backbone amide 15N chemical shifts of the same and the next residue. These experiments exploit a by far superior dispersion of backbone amide 15N chemical shifts, and permit unambiguous assignments of all Asn/Gln side-chain NH2 groups in the intrinsically disordered protein α-synuclein and the majority of Gln NH2 groups in the disordered huntington exon-1 protein with a 7-residue glutamine repeat, httex1Q7.
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