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Updated: Nov 24, 2025

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
Carbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening:
Yuichi Yoshimura1, Masatomo So2, Yohei Miyanoiri2
1Institute for Protein Research, Osaka University, Yamada-oka 3-2, Suita, 565-0871 Osaka, Japan; Program of Mathematical and Life Sciences, Graduate School of Integrated Sciences for Life, Hiroshima University, Kagamiyama 1-3-1, Higashi-Hiroshima, 739-8526 Hiroshima, Japan; Lifematics West-Japan Branch, Hirano-machi 4-6-16, Chuo-ku, 541-0046 Osaka, Japan.
Abstract:
The 15N-1H heteronuclear single-quantum correlation (HSQC) technique in protein NMR spectroscopy suffers from line-broadening effects, such as chemical exchange of labile protons with solvent, and exchange broadening for residues undergoing conformational dynamics. The amide resonance of β2-microglobulin residue S88 is not observed in the HSQC spectrum but can be obtained through 13C-detect experiments that circumvent the problem of amide-solvent exchange broadening. Line broadening of S88 resonance beyond detection in the HSQC spectrum is not attributed to conformational exchange but rather to solvent exchange occurring on the order of ~103 s-1.
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