Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway

Studying the unfolding of membrane proteins in a native-like lipid environment is challenging. Here the authors describe a method combining hydrogen-deuterium exchange and solid-state NMR measurements that allows the characterization of unfolding events in lipid-embedded membrane proteins and use th...

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Autores principales:	Peng Xiao, David Bolton, Rachel A. Munro, Leonid S. Brown, Vladimir Ladizhansky
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/598def11c2fc4bcd97e663bc018acd2a
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spelling	oai:doaj.org-article:598def11c2fc4bcd97e663bc018acd2a2021-12-02T16:58:15ZSolid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway10.1038/s41467-019-11849-82041-1723https://doaj.org/article/598def11c2fc4bcd97e663bc018acd2a2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11849-8https://doaj.org/toc/2041-1723Studying the unfolding of membrane proteins in a native-like lipid environment is challenging. Here the authors describe a method combining hydrogen-deuterium exchange and solid-state NMR measurements that allows the characterization of unfolding events in lipid-embedded membrane proteins and use the photoreceptor Anabaena Sensory Rhodopsin as a test case.Peng XiaoDavid BoltonRachel A. MunroLeonid S. BrownVladimir LadizhanskyNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Peng Xiao David Bolton Rachel A. Munro Leonid S. Brown Vladimir Ladizhansky Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
description	Studying the unfolding of membrane proteins in a native-like lipid environment is challenging. Here the authors describe a method combining hydrogen-deuterium exchange and solid-state NMR measurements that allows the characterization of unfolding events in lipid-embedded membrane proteins and use the photoreceptor Anabaena Sensory Rhodopsin as a test case.
format	article
author	Peng Xiao David Bolton Rachel A. Munro Leonid S. Brown Vladimir Ladizhansky
author_facet	Peng Xiao David Bolton Rachel A. Munro Leonid S. Brown Vladimir Ladizhansky
author_sort	Peng Xiao
title	Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
title_short	Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
title_full	Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
title_fullStr	Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
title_full_unstemmed	Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
title_sort	solid-state nmr spectroscopy based atomistic view of a membrane protein unfolding pathway
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/598def11c2fc4bcd97e663bc018acd2a
work_keys_str_mv	AT pengxiao solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway AT davidbolton solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway AT rachelamunro solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway AT leonidsbrown solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway AT vladimirladizhansky solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway
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Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway

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