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Updated: Aug 19, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Through-bond heteronuclear single-quantum correlation spectroscopy in solid-state NMR, and comparison to other
1Laboratoire de Stéréochimie et des Interactions Moléculaires, UMR-117 CNRS/ENS, Ecole Normale Supérieure de Lyon, 69364 Lyon, France.
Abstract:
A new through-bond carbon-proton correlation technique, the MAS-J-HSQC experiment, is described for solid-state NMR. This new pulse scheme is compared experimentally with the previously proposed MAS-J-HMQC experiment in terms of proton resolution on a model sample of powdered L-alanine. We show that for natural abundance compounds, the MAS-J-HMQC and MAS-J-HSQC experiments give about the same proton resolution, whereas, for (13)C-labeled materials, narrower proton linewidths are obtained with the MAS-J-HSQC experiment. In addition we show that in scalar as well as in dipolar heteronuclear shift correlation experiments, when the proton chemical shift is encoded by the evolution of a single-quantum coherence, the proton resolution can be enhanced by simply adding a 180 degrees carbon pulse in the middle of the t(1) evolution time.
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