In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code

The membrane transporter BtuB is site-directedly spin labelled on the surface of living Escherichia coli via Diels–Alder click chemistry of the genetically encoded amino acid SCO-l-lysine. The previously introduced photoactivatable nitroxide PaNDA prevents off-target labelling, is used for distance...

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Autores principales: Kugele, Anandi, Ketter, Sophie, Silkenath, Bjarne, Wittmann, Valentin, Joseph, Benesh, Drescher, Malte
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8640571/
https://www.ncbi.nlm.nih.gov/pubmed/34792069
http://dx.doi.org/10.1039/d1cc04612h
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author Kugele, Anandi
Ketter, Sophie
Silkenath, Bjarne
Wittmann, Valentin
Joseph, Benesh
Drescher, Malte
author_facet Kugele, Anandi
Ketter, Sophie
Silkenath, Bjarne
Wittmann, Valentin
Joseph, Benesh
Drescher, Malte
author_sort Kugele, Anandi
collection PubMed
description The membrane transporter BtuB is site-directedly spin labelled on the surface of living Escherichia coli via Diels–Alder click chemistry of the genetically encoded amino acid SCO-l-lysine. The previously introduced photoactivatable nitroxide PaNDA prevents off-target labelling, is used for distance measurements, and the temporally shifted activation of the nitroxide allows for advanced experimental setups. This study describes significant evolution of Diels–Alder-mediated spin labelling on cellular surfaces and opens up new vistas for the the study of membrane proteins.
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spelling pubmed-86405712021-12-30 In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code Kugele, Anandi Ketter, Sophie Silkenath, Bjarne Wittmann, Valentin Joseph, Benesh Drescher, Malte Chem Commun (Camb) Chemistry The membrane transporter BtuB is site-directedly spin labelled on the surface of living Escherichia coli via Diels–Alder click chemistry of the genetically encoded amino acid SCO-l-lysine. The previously introduced photoactivatable nitroxide PaNDA prevents off-target labelling, is used for distance measurements, and the temporally shifted activation of the nitroxide allows for advanced experimental setups. This study describes significant evolution of Diels–Alder-mediated spin labelling on cellular surfaces and opens up new vistas for the the study of membrane proteins. The Royal Society of Chemistry 2021-11-18 /pmc/articles/PMC8640571/ /pubmed/34792069 http://dx.doi.org/10.1039/d1cc04612h Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Kugele, Anandi
Ketter, Sophie
Silkenath, Bjarne
Wittmann, Valentin
Joseph, Benesh
Drescher, Malte
In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code
title In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code
title_full In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code
title_fullStr In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code
title_full_unstemmed In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code
title_short In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code
title_sort in situ epr spectroscopy of a bacterial membrane transporter using an expanded genetic code
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8640571/
https://www.ncbi.nlm.nih.gov/pubmed/34792069
http://dx.doi.org/10.1039/d1cc04612h
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