Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Bayer, Peter, Matena, Anja, Beuck, Christine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Beilstein-Institut 2020
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
_version_ 1783593829450907648
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
work_keys_str_mv AT bayerpeter nmrspectroscopyofsupramolecularchemistryonproteinsurfaces
AT matenaanja nmrspectroscopyofsupramolecularchemistryonproteinsurfaces
AT beuckchristine nmrspectroscopyofsupramolecularchemistryonproteinsurfaces