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231224s2015 xx |||||o 00| ||eng c |
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|a 10.1016/j.pnmrs.2015.02.002
|2 doi
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|a eng
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|a Zangger, Klaus
|e verfasserin
|4 aut
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|a Pure shift NMR
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|c 2015
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 11.04.2016
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|a Date Revised 14.02.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2015 The Author. Published by Elsevier B.V. All rights reserved.
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a Homonuclear broadband decoupling
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|a NMR spectroscopy
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|a Pure shift NMR
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|a Scalar coupling
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|a Structure analysis
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|a Carbon Isotopes
|2 NLM
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|a Proteins
|2 NLM
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|i Enthalten in
|t Progress in nuclear magnetic resonance spectroscopy
|d 1998
|g 86-87(2015) vom: 28. Apr., Seite 1-20
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|x 1873-3301
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|g volume:86-87
|g year:2015
|g day:28
|g month:04
|g pages:1-20
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|u http://dx.doi.org/10.1016/j.pnmrs.2015.02.002
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