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Pure-Shift NMR

  • Walter Becker
  • Nina Gubensäk
  • Klaus Zangger
Reference work entry

Abstract

The signal dispersion in one- and multidimensional NMR spectra of organic and biomolecules is limited by the low resolution in the proton dimension. This results from both the limited proton chemical shift range but also signal splitting by scalar coupling. Pure-shift NMR by homonuclear broadband decoupling has been introduced as a way of simplifying spectra in the proton dimension by collapsing all signals into singlets. Although the acquisition of pure shift spectra has been attempted since the early days of solution NMR, the recent progress in pulse-sequence design finally enabled their straightforward acquisition in routine NMR labs. Interrupted-acquisition experiments allow the recording of quantitative real-time pure-shift spectra without sophisticated data processing. Pure-shift spectra are especially useful for highly overlapped proton spectra, as found for example in natural products, reaction mixtures, and biomacromolecules. The increase in resolution comes however at the prize of a significant reduction in sensitivity, since actual broadband homonuclear decoupling can only be achieved for a subset of spins.

Keywords

NMR spectroscopy Pure-shift NMR Structure analysis Proton NMR Scalar coupling Homonuclear broadband decoupling 

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Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Institute of ChemistryUniversity of GrazGrazAustria

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