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DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells

Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid‐state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high‐sensiti...

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Autores principales: Narasimhan, Siddarth, Scherpe, Stephan, Lucini Paioni, Alessandra, van der Zwan, Johan, Folkers, Gert E., Ovaa, Huib, Baldus, Marc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772113/
https://www.ncbi.nlm.nih.gov/pubmed/31233270
http://dx.doi.org/10.1002/anie.201903246
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author Narasimhan, Siddarth
Scherpe, Stephan
Lucini Paioni, Alessandra
van der Zwan, Johan
Folkers, Gert E.
Ovaa, Huib
Baldus, Marc
author_facet Narasimhan, Siddarth
Scherpe, Stephan
Lucini Paioni, Alessandra
van der Zwan, Johan
Folkers, Gert E.
Ovaa, Huib
Baldus, Marc
author_sort Narasimhan, Siddarth
collection PubMed
description Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid‐state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high‐sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in‐cell solution‐state NMR spectroscopy due to molecular size limitations.
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spelling pubmed-67721132019-10-07 DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells Narasimhan, Siddarth Scherpe, Stephan Lucini Paioni, Alessandra van der Zwan, Johan Folkers, Gert E. Ovaa, Huib Baldus, Marc Angew Chem Int Ed Engl Communications Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid‐state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high‐sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in‐cell solution‐state NMR spectroscopy due to molecular size limitations. John Wiley and Sons Inc. 2019-07-19 2019-09-09 /pmc/articles/PMC6772113/ /pubmed/31233270 http://dx.doi.org/10.1002/anie.201903246 Text en © 2019 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-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Communications
Narasimhan, Siddarth
Scherpe, Stephan
Lucini Paioni, Alessandra
van der Zwan, Johan
Folkers, Gert E.
Ovaa, Huib
Baldus, Marc
DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells
title DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells
title_full DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells
title_fullStr DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells
title_full_unstemmed DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells
title_short DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells
title_sort dnp‐supported solid‐state nmr spectroscopy of proteins inside mammalian cells
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772113/
https://www.ncbi.nlm.nih.gov/pubmed/31233270
http://dx.doi.org/10.1002/anie.201903246
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