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Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1

(19)F NMR protein observed spectroscopy is evaluated as a method for analysing protein metal binding using the New Delhi metallo-β-lactamase 1. The results imply (19)F NMR is useful for analysis of different metallated protein states and investigations on equilibrium states in the presence of inhibi...

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Autores principales: Rydzik, Anna M., Brem, Jürgen, Chandler, Shane A., Benesch, Justin L. P., Claridge, Timothy D. W., Schofield, Christopher J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7484990/
https://www.ncbi.nlm.nih.gov/pubmed/33479644
http://dx.doi.org/10.1039/c9md00416e
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author Rydzik, Anna M.
Brem, Jürgen
Chandler, Shane A.
Benesch, Justin L. P.
Claridge, Timothy D. W.
Schofield, Christopher J.
author_facet Rydzik, Anna M.
Brem, Jürgen
Chandler, Shane A.
Benesch, Justin L. P.
Claridge, Timothy D. W.
Schofield, Christopher J.
author_sort Rydzik, Anna M.
collection PubMed
description (19)F NMR protein observed spectroscopy is evaluated as a method for analysing protein metal binding using the New Delhi metallo-β-lactamase 1. The results imply (19)F NMR is useful for analysis of different metallated protein states and investigations on equilibrium states in the presence of inhibitors. One limitation is that (19)F labelling may affect metal ion binding. The sensitive readout of changes in protein behaviour observed by (19)F NMR spectra coupled with the broad scope of tolerated conditions (e.g. buffer variations) means (19)F NMR should be further investigated for studying metal ion interactions and the inhibition of metallo-enzymes during drug discovery.
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spelling pubmed-74849902020-10-02 Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1 Rydzik, Anna M. Brem, Jürgen Chandler, Shane A. Benesch, Justin L. P. Claridge, Timothy D. W. Schofield, Christopher J. RSC Med Chem Chemistry (19)F NMR protein observed spectroscopy is evaluated as a method for analysing protein metal binding using the New Delhi metallo-β-lactamase 1. The results imply (19)F NMR is useful for analysis of different metallated protein states and investigations on equilibrium states in the presence of inhibitors. One limitation is that (19)F labelling may affect metal ion binding. The sensitive readout of changes in protein behaviour observed by (19)F NMR spectra coupled with the broad scope of tolerated conditions (e.g. buffer variations) means (19)F NMR should be further investigated for studying metal ion interactions and the inhibition of metallo-enzymes during drug discovery. Royal Society of Chemistry 2020-02-21 /pmc/articles/PMC7484990/ /pubmed/33479644 http://dx.doi.org/10.1039/c9md00416e Text en This journal is © The Royal Society of Chemistry 2020 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Rydzik, Anna M.
Brem, Jürgen
Chandler, Shane A.
Benesch, Justin L. P.
Claridge, Timothy D. W.
Schofield, Christopher J.
Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1
title Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1
title_full Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1
title_fullStr Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1
title_full_unstemmed Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1
title_short Monitoring protein-metal binding by (19)F NMR – a case study with the New Delhi metallo-β-lactamase 1
title_sort monitoring protein-metal binding by (19)f nmr – a case study with the new delhi metallo-β-lactamase 1
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7484990/
https://www.ncbi.nlm.nih.gov/pubmed/33479644
http://dx.doi.org/10.1039/c9md00416e
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