Pure shift NMR
Copyright © 2015 The Author. Published by Elsevier B.V. All rights reserved.
| Veröffentlicht in: | Progress in nuclear magnetic resonance spectroscopy. - 1998. - 86-87(2015) vom: 28. Apr., Seite 1-20 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2015
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| Zugriff auf das übergeordnete Werk: | Progress in nuclear magnetic resonance spectroscopy |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Review Homonuclear broadband decoupling NMR spectroscopy Pure shift NMR Scalar coupling Structure analysis Carbon Isotopes Proteins |
| Zusammenfassung: | Copyright © 2015 The Author. Published by Elsevier B.V. All rights reserved. Although scalar-coupling provides important structural information, the resulting signal splittings significantly reduce the resolution of NMR spectra. Limited resolution is a particular problem in proton NMR experiments, resulting in part from the limited proton chemical shift range (∼10 ppm) but even more from the splittings due to scalar coupling to nearby protons. "Pure shift" NMR spectroscopy (also known as broadband homonuclear decoupling) has been developed for disentangling overlapped proton NMR spectra. The resulting spectra are considerably simplified as they consist of single lines, reminiscent of proton-decoupled C-13 spectra at natural abundance, with no multiplet structure. The different approaches to obtaining pure shift spectra are reviewed here and several applications presented. Pure shift spectra are especially useful for highly overlapped proton spectra, as found for example in reaction mixtures, natural products and biomacromolecules |
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| Beschreibung: | Date Completed 11.04.2016 Date Revised 14.02.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-3301 |
| DOI: | 10.1016/j.pnmrs.2015.02.002 |