Rapid analysis of isotopically unmodified amino acids by high-resolution N-14-edited H-1-C-13 correlation NMR spectroscopy - Université de Lille
Article Dans Une Revue Chemical Communications Année : 2008

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

Résumé

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

Domaines

Chimie

Dates et versions

hal-04558860 , version 1 (25-04-2024)

Identifiants

Citer

Jean-Paul Amoureux, Qiang Wang, Bingwen Hu, Olivier Lafon, Julien Trebosc, et al.. Rapid analysis of isotopically unmodified amino acids by high-resolution N-14-edited H-1-C-13 correlation NMR spectroscopy. Chemical Communications, 2008, Chemical Communications, -, pp.6525-6527. ⟨10.1039/b816362f⟩. ⟨hal-04558860⟩
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