Structure of outer membrane protein G in lipid bilayers

Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.

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Autores principales:	Joren S. Retel, Andrew J. Nieuwkoop, Matthias Hiller, Victoria A. Higman, Emeline Barbet-Massin, Jan Stanek, Loren B. Andreas, W. Trent Franks, Barth-Jan van Rossum, Kutti R. Vinothkumar, Lieselotte Handel, Gregorio Giuseppe de Palma, Benjamin Bardiaux, Guido Pintacuda, Lyndon Emsley, Werner Kühlbrandt, Hartmut Oschkinat
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b2819bbf534e44df99c9109dd893ff55
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spelling	oai:doaj.org-article:b2819bbf534e44df99c9109dd893ff552021-12-02T14:41:00ZStructure of outer membrane protein G in lipid bilayers10.1038/s41467-017-02228-22041-1723https://doaj.org/article/b2819bbf534e44df99c9109dd893ff552017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02228-2https://doaj.org/toc/2041-1723Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.Joren S. RetelAndrew J. NieuwkoopMatthias HillerVictoria A. HigmanEmeline Barbet-MassinJan StanekLoren B. AndreasW. Trent FranksBarth-Jan van RossumKutti R. VinothkumarLieselotte HandelGregorio Giuseppe de PalmaBenjamin BardiauxGuido PintacudaLyndon EmsleyWerner KühlbrandtHartmut OschkinatNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joren S. Retel Andrew J. Nieuwkoop Matthias Hiller Victoria A. Higman Emeline Barbet-Massin Jan Stanek Loren B. Andreas W. Trent Franks Barth-Jan van Rossum Kutti R. Vinothkumar Lieselotte Handel Gregorio Giuseppe de Palma Benjamin Bardiaux Guido Pintacuda Lyndon Emsley Werner Kühlbrandt Hartmut Oschkinat Structure of outer membrane protein G in lipid bilayers
description	Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.
format	article
author	Joren S. Retel Andrew J. Nieuwkoop Matthias Hiller Victoria A. Higman Emeline Barbet-Massin Jan Stanek Loren B. Andreas W. Trent Franks Barth-Jan van Rossum Kutti R. Vinothkumar Lieselotte Handel Gregorio Giuseppe de Palma Benjamin Bardiaux Guido Pintacuda Lyndon Emsley Werner Kühlbrandt Hartmut Oschkinat
author_facet	Joren S. Retel Andrew J. Nieuwkoop Matthias Hiller Victoria A. Higman Emeline Barbet-Massin Jan Stanek Loren B. Andreas W. Trent Franks Barth-Jan van Rossum Kutti R. Vinothkumar Lieselotte Handel Gregorio Giuseppe de Palma Benjamin Bardiaux Guido Pintacuda Lyndon Emsley Werner Kühlbrandt Hartmut Oschkinat
author_sort	Joren S. Retel
title	Structure of outer membrane protein G in lipid bilayers
title_short	Structure of outer membrane protein G in lipid bilayers
title_full	Structure of outer membrane protein G in lipid bilayers
title_fullStr	Structure of outer membrane protein G in lipid bilayers
title_full_unstemmed	Structure of outer membrane protein G in lipid bilayers
title_sort	structure of outer membrane protein g in lipid bilayers
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/b2819bbf534e44df99c9109dd893ff55
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Structure of outer membrane protein G in lipid bilayers

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