1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement

A 1H anisotropic-isotropic chemical shift correlation experiment which employs symmetry-based recoupling sequences to reintroduce the chemical shift anisotropy in ν1 and ultrafast MAS to resolve 1H sites in ν2 is described. This experiment is used to measure 1H shift parameters for L-ascorbic acid,...

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Main Authors: Miah, Habeeba K., Cresswell, Rosalie, Iuga, Dinu, Titman, Jeremy J.
Format: Article
Published: Elsevier 2017
Online Access:https://eprints.nottingham.ac.uk/40628/
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author Miah, Habeeba K.
Cresswell, Rosalie
Iuga, Dinu
Titman, Jeremy J.
author_facet Miah, Habeeba K.
Cresswell, Rosalie
Iuga, Dinu
Titman, Jeremy J.
author_sort Miah, Habeeba K.
building Nottingham Research Data Repository
collection Online Access
description A 1H anisotropic-isotropic chemical shift correlation experiment which employs symmetry-based recoupling sequences to reintroduce the chemical shift anisotropy in ν1 and ultrafast MAS to resolve 1H sites in ν2 is described. This experiment is used to measure 1H shift parameters for L-ascorbic acid, a compound with a relatively complex hydrogen-bonding network in the solid. The 1H CSAs of hydrogen-bonded sites with resolved isotropic shifts can be extracted directly from the recoupled lineshapes. In combination with DFT calculations, hydrogen positions in crystal structures obtained from X-ray and neutron diffraction are refined by comparison with simulations of the full two-dimensional NMR spectrum. The improved resolution afforded by the second dimension allows even unresolved hydrogen-bonded sites 1H to be assigned and their shift parameters to be obtained.
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institution University of Nottingham Malaysia Campus
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spelling nottingham-406282020-05-04T18:34:58Z https://eprints.nottingham.ac.uk/40628/ 1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement Miah, Habeeba K. Cresswell, Rosalie Iuga, Dinu Titman, Jeremy J. A 1H anisotropic-isotropic chemical shift correlation experiment which employs symmetry-based recoupling sequences to reintroduce the chemical shift anisotropy in ν1 and ultrafast MAS to resolve 1H sites in ν2 is described. This experiment is used to measure 1H shift parameters for L-ascorbic acid, a compound with a relatively complex hydrogen-bonding network in the solid. The 1H CSAs of hydrogen-bonded sites with resolved isotropic shifts can be extracted directly from the recoupled lineshapes. In combination with DFT calculations, hydrogen positions in crystal structures obtained from X-ray and neutron diffraction are refined by comparison with simulations of the full two-dimensional NMR spectrum. The improved resolution afforded by the second dimension allows even unresolved hydrogen-bonded sites 1H to be assigned and their shift parameters to be obtained. Elsevier 2017-02-13 Article PeerReviewed Miah, Habeeba K., Cresswell, Rosalie, Iuga, Dinu and Titman, Jeremy J. (2017) 1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement. Solid-State Nuclear Magnetic Resonance . ISSN 1527-3326 (In Press) http://www.sciencedirect.com/science/article/pii/S0926204016301515 doi:10.1016/j.ssnmr.2017.02.002 doi:10.1016/j.ssnmr.2017.02.002
spellingShingle Miah, Habeeba K.
Cresswell, Rosalie
Iuga, Dinu
Titman, Jeremy J.
1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement
title 1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement
title_full 1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement
title_fullStr 1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement
title_full_unstemmed 1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement
title_short 1H CSA parameters by ultrafast MAS NMR: measurement and applications to structure refinement
title_sort 1h csa parameters by ultrafast mas nmr: measurement and applications to structure refinement
url https://eprints.nottingham.ac.uk/40628/
https://eprints.nottingham.ac.uk/40628/
https://eprints.nottingham.ac.uk/40628/