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NMR Spectroscopy of supramolecular chemistry on protein surfaces
As one of the few analytical methods that offer atomic resolution, NMR spectroscopy is a valuable tool to study the interaction of proteins with their interaction partners, both biomolecules and synthetic ligands. In recent years, the focus in chemistry has kept expanding from targeting small bindin...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Beilstein-Institut
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7554676/ https://www.ncbi.nlm.nih.gov/pubmed/33093929 http://dx.doi.org/10.3762/bjoc.16.203 |
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author | Bayer, Peter Matena, Anja Beuck, Christine |
author_facet | Bayer, Peter Matena, Anja Beuck, Christine |
author_sort | Bayer, Peter |
collection | PubMed |
description | As one of the few analytical methods that offer atomic resolution, NMR spectroscopy is a valuable tool to study the interaction of proteins with their interaction partners, both biomolecules and synthetic ligands. In recent years, the focus in chemistry has kept expanding from targeting small binding pockets in proteins to recognizing patches on protein surfaces, mostly via supramolecular chemistry, with the goal to modulate protein–protein interactions. Here we present NMR methods that have been applied to characterize these molecular interactions and discuss the challenges of this endeavor. |
format | Online Article Text |
id | pubmed-7554676 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Beilstein-Institut |
record_format | MEDLINE/PubMed |
spelling | pubmed-75546762020-10-21 NMR Spectroscopy of supramolecular chemistry on protein surfaces Bayer, Peter Matena, Anja Beuck, Christine Beilstein J Org Chem Review As one of the few analytical methods that offer atomic resolution, NMR spectroscopy is a valuable tool to study the interaction of proteins with their interaction partners, both biomolecules and synthetic ligands. In recent years, the focus in chemistry has kept expanding from targeting small binding pockets in proteins to recognizing patches on protein surfaces, mostly via supramolecular chemistry, with the goal to modulate protein–protein interactions. Here we present NMR methods that have been applied to characterize these molecular interactions and discuss the challenges of this endeavor. Beilstein-Institut 2020-10-09 /pmc/articles/PMC7554676/ /pubmed/33093929 http://dx.doi.org/10.3762/bjoc.16.203 Text en Copyright © 2020, Bayer et al. https://creativecommons.org/licenses/by/4.0https://www.beilstein-journals.org/bjoc/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0). Please note that the reuse, redistribution and reproduction in particular requires that the authors and source are credited. The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms) |
spellingShingle | Review Bayer, Peter Matena, Anja Beuck, Christine NMR Spectroscopy of supramolecular chemistry on protein surfaces |
title | NMR Spectroscopy of supramolecular chemistry on protein surfaces |
title_full | NMR Spectroscopy of supramolecular chemistry on protein surfaces |
title_fullStr | NMR Spectroscopy of supramolecular chemistry on protein surfaces |
title_full_unstemmed | NMR Spectroscopy of supramolecular chemistry on protein surfaces |
title_short | NMR Spectroscopy of supramolecular chemistry on protein surfaces |
title_sort | nmr spectroscopy of supramolecular chemistry on protein surfaces |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7554676/ https://www.ncbi.nlm.nih.gov/pubmed/33093929 http://dx.doi.org/10.3762/bjoc.16.203 |
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