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XLSY: Extra‐Large NMR Spectroscopy

NMR studies of intrinsically disordered proteins and other complex biomolecular systems require spectra with the highest resolution and dimensionality. An efficient approach, extra‐large NMR spectroscopy, is presented for experimental data collection, reconstruction, and handling of very large NMR s...

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Detalles Bibliográficos
Autores principales: Pustovalova, Yulia, Mayzel, Maxim, Orekhov, Vladislav Yu.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6585689/
https://www.ncbi.nlm.nih.gov/pubmed/30175546
http://dx.doi.org/10.1002/anie.201806144
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author Pustovalova, Yulia
Mayzel, Maxim
Orekhov, Vladislav Yu.
author_facet Pustovalova, Yulia
Mayzel, Maxim
Orekhov, Vladislav Yu.
author_sort Pustovalova, Yulia
collection PubMed
description NMR studies of intrinsically disordered proteins and other complex biomolecular systems require spectra with the highest resolution and dimensionality. An efficient approach, extra‐large NMR spectroscopy, is presented for experimental data collection, reconstruction, and handling of very large NMR spectra by a combination of the radial and non‐uniform sampling, a new processing algorithm, and rigorous statistical validation. We demonstrate the first high‐quality reconstruction of a full seven‐dimensional HNCOCACONH and two five‐dimensional HACACONH and HN(CA)CONH experiments for a representative intrinsically disordered protein α‐synuclein. XLSY will significantly enhance the NMR toolbox in challenging biomolecular studies.
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spelling pubmed-65856892019-06-27 XLSY: Extra‐Large NMR Spectroscopy Pustovalova, Yulia Mayzel, Maxim Orekhov, Vladislav Yu. Angew Chem Int Ed Engl Communications NMR studies of intrinsically disordered proteins and other complex biomolecular systems require spectra with the highest resolution and dimensionality. An efficient approach, extra‐large NMR spectroscopy, is presented for experimental data collection, reconstruction, and handling of very large NMR spectra by a combination of the radial and non‐uniform sampling, a new processing algorithm, and rigorous statistical validation. We demonstrate the first high‐quality reconstruction of a full seven‐dimensional HNCOCACONH and two five‐dimensional HACACONH and HN(CA)CONH experiments for a representative intrinsically disordered protein α‐synuclein. XLSY will significantly enhance the NMR toolbox in challenging biomolecular studies. John Wiley and Sons Inc. 2018-10-01 2018-10-22 /pmc/articles/PMC6585689/ /pubmed/30175546 http://dx.doi.org/10.1002/anie.201806144 Text en © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Communications
Pustovalova, Yulia
Mayzel, Maxim
Orekhov, Vladislav Yu.
XLSY: Extra‐Large NMR Spectroscopy
title XLSY: Extra‐Large NMR Spectroscopy
title_full XLSY: Extra‐Large NMR Spectroscopy
title_fullStr XLSY: Extra‐Large NMR Spectroscopy
title_full_unstemmed XLSY: Extra‐Large NMR Spectroscopy
title_short XLSY: Extra‐Large NMR Spectroscopy
title_sort xlsy: extra‐large nmr spectroscopy
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6585689/
https://www.ncbi.nlm.nih.gov/pubmed/30175546
http://dx.doi.org/10.1002/anie.201806144
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