Rapid analysis of isotopically unmodified amino acids by high-resolution 14N-edited 1H–13C correlation NMR spectroscopy

Jean-Paul Amoureux; Qiang Wang; Bingwen Hu; Olivier Lafon; Julien Trébosc; Feng Deng

doi:10.1039/B816362F

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Rapid analysis of isotopically unmodified amino acids by high-resolution ¹⁴N-edited ¹H–¹³C correlation NMR spectroscopy†

Jean-Paul Amoureux,*^a Qiang Wang,^abc Bingwen Hu,^a Olivier Lafon,^a Julien Trébosc^a and Feng Deng^b

Author affiliations

* Corresponding authors

^a UCCS (CNRS-8181), University of Lille, Villeneuve d’Ascq, France
E-mail: jean-paul.amoureux@univ-lille1.fr
Fax: 33 320436814
Tel: 33 320434143

^b State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, P. R. China

^c Graduate School of the Chinese Academy of Sciences, Beijing, P. R. China

Abstract

A ¹⁴N-edited ¹H–¹³C NMR method is described for structural analysis under high-resolution of biomolecules without any enrichment.

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Supplementary files

Fig. 3: L-glutamine. (a) Molecular structure with atomlabelling matching IUPAC recommendations. (b, c) CPHETCOR spectrawith: (b) all (S₀) or (c) ¹⁴N-edited (S₀ − S₁) ¹H–¹³C cross-peaks PDF (255K)

Article information

DOI: https://doi.org/10.1039/B816362F
Article type: Communication
Submitted: 17 Sep 2008
Accepted: 10 Oct 2008
First published: 07 Nov 2008

Download Citation

Chem. Commun., 2008, 6525-6527

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Rapid analysis of isotopically unmodified amino acids by high-resolution ¹⁴N-edited ¹H–¹³C correlation NMR spectroscopy

J. Amoureux, Q. Wang, B. Hu, O. Lafon, J. Trébosc and F. Deng, Chem. Commun., 2008, 6525 DOI: 10.1039/B816362F

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