Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy

Proton detection and fast magic‐angle spinning have advanced biological solid‐state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no method has been proposed to detect intermolecular interfaces in these assemblies by pro...

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Detalles Bibliográficos
Autores principales: Zinke, Maximilian, Fricke, Pascal, Lange, Sascha, Zinn‐Justin, Sophie, Lange, Adam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6220863/
https://www.ncbi.nlm.nih.gov/pubmed/29917302
http://dx.doi.org/10.1002/cphc.201800542
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author Zinke, Maximilian
Fricke, Pascal
Lange, Sascha
Zinn‐Justin, Sophie
Lange, Adam
author_facet Zinke, Maximilian
Fricke, Pascal
Lange, Sascha
Zinn‐Justin, Sophie
Lange, Adam
author_sort Zinke, Maximilian
collection PubMed
description Proton detection and fast magic‐angle spinning have advanced biological solid‐state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no method has been proposed to detect intermolecular interfaces in these assemblies by proton detection. Herein, we introduce a concept based on methyl labeling that allows for the assignment of these moieties and for the study of protein−protein interfaces at atomic resolution.
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spelling pubmed-62208632018-11-13 Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy Zinke, Maximilian Fricke, Pascal Lange, Sascha Zinn‐Justin, Sophie Lange, Adam Chemphyschem Communications Proton detection and fast magic‐angle spinning have advanced biological solid‐state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no method has been proposed to detect intermolecular interfaces in these assemblies by proton detection. Herein, we introduce a concept based on methyl labeling that allows for the assignment of these moieties and for the study of protein−protein interfaces at atomic resolution. John Wiley and Sons Inc. 2018-06-27 2018-10-05 /pmc/articles/PMC6220863/ /pubmed/29917302 http://dx.doi.org/10.1002/cphc.201800542 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-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
Zinke, Maximilian
Fricke, Pascal
Lange, Sascha
Zinn‐Justin, Sophie
Lange, Adam
Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy
title Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy
title_full Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy
title_fullStr Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy
title_full_unstemmed Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy
title_short Protein−Protein Interfaces Probed by Methyl Labeling and Proton‐Detected Solid‐State NMR Spectroscopy
title_sort protein−protein interfaces probed by methyl labeling and proton‐detected solid‐state nmr spectroscopy
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6220863/
https://www.ncbi.nlm.nih.gov/pubmed/29917302
http://dx.doi.org/10.1002/cphc.201800542
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