Abstract
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.
Hybrid polarizing solids for pure hyperpolarized liquids through dissolution dynamic nuclear polarization
From The DNP-NMR Blog:
Hybrid polarizing solids for pure hyperpolarized liquids through dissolution dynamic nuclear polarization
Gajan, D., et al., Hybrid polarizing solids for pure hyperpolarized liquids through dissolution dynamic nuclear polarization. Proc. Nat. Aca. Sci. USA, 2014. 111(41): p. 14693-14697.
http://www.pnas.org/content/111/41/14693.abstract
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08-17-2015 07:21 PM
Pure shift NMR
Pure shift NMR
Publication date: April 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volumes 86–87</br>
Author(s): Klaus Zangger</br>
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 (~10ppm) but even more from the splittings due to scalar coupling to nearby protons. “Pure shift” NMR spectroscopy (also known as...
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04-12-2015 02:40 AM
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Abstract
Spectral resolution in proton NMR spectroscopy is reduced by the splitting of resonances into multiplets due to the effect of homonuclear scalar couplings. Although these effects are often hidden in protein NMR spectroscopy by low digital resolution and routine apodization, behind the scenes homonuclear scalar couplings increase spectral overcrowding. The possibilities for biomolecular NMR offered by new pure shift NMR methods are illustrated here....
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03-04-2015 08:56 AM
[NMR paper] Improved pulse sequences for pure exchange solid-state NMR spectroscopy.
Improved pulse sequences for pure exchange solid-state NMR spectroscopy.
Related Articles Improved pulse sequences for pure exchange solid-state NMR spectroscopy.
Magn Reson Chem. 2004 Feb;42(2):285-90
Authors: Vosegaard T, Nielsen NC
Spin-exchange experiments are useful for improving the resolution and establishment of sequential assignments in solid-state NMR spectra of uniformly (15)N-labeled proteins oriented macroscopically in phospholipid bilayers. To exploit this advantage fully, it is crucial that the diagonal peaks in the...
Pure shift NMR.
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