Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation

Through neutron reflectometry and NMR spectroscopy studies, Mushtaq et al study the full-length Bcl-2 protein reconstituted in lipid bilayers. They find that, in contrast to previously studied truncated, soluble protein versions, intact Bcl-2 is mainly embedded in the membrane with its regulatory lo...

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Autores principales:	Ameeq Ul Mushtaq, Jörgen Ådén, Luke A. Clifton, Hanna Wacklin-Knecht, Mario Campana, Artur P. G. Dingeldein, Cecilia Persson, Tobias Sparrman, Gerhard Gröbner
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/04e38e0553dd4095833d3e485d2fc850
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spelling	oai:doaj.org-article:04e38e0553dd4095833d3e485d2fc8502021-12-02T17:15:15ZNeutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation10.1038/s42003-021-02032-12399-3642https://doaj.org/article/04e38e0553dd4095833d3e485d2fc8502021-04-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02032-1https://doaj.org/toc/2399-3642Through neutron reflectometry and NMR spectroscopy studies, Mushtaq et al study the full-length Bcl-2 protein reconstituted in lipid bilayers. They find that, in contrast to previously studied truncated, soluble protein versions, intact Bcl-2 is mainly embedded in the membrane with its regulatory loop highly flexible.Ameeq Ul MushtaqJörgen ÅdénLuke A. CliftonHanna Wacklin-KnechtMario CampanaArtur P. G. DingeldeinCecilia PerssonTobias SparrmanGerhard GröbnerNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Ameeq Ul Mushtaq Jörgen Ådén Luke A. Clifton Hanna Wacklin-Knecht Mario Campana Artur P. G. Dingeldein Cecilia Persson Tobias Sparrman Gerhard Gröbner Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
description	Through neutron reflectometry and NMR spectroscopy studies, Mushtaq et al study the full-length Bcl-2 protein reconstituted in lipid bilayers. They find that, in contrast to previously studied truncated, soluble protein versions, intact Bcl-2 is mainly embedded in the membrane with its regulatory loop highly flexible.
format	article
author	Ameeq Ul Mushtaq Jörgen Ådén Luke A. Clifton Hanna Wacklin-Knecht Mario Campana Artur P. G. Dingeldein Cecilia Persson Tobias Sparrman Gerhard Gröbner
author_facet	Ameeq Ul Mushtaq Jörgen Ådén Luke A. Clifton Hanna Wacklin-Knecht Mario Campana Artur P. G. Dingeldein Cecilia Persson Tobias Sparrman Gerhard Gröbner
author_sort	Ameeq Ul Mushtaq
title	Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
title_short	Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
title_full	Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
title_fullStr	Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
title_full_unstemmed	Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
title_sort	neutron reflectometry and nmr spectroscopy of full-length bcl-2 protein reveal its membrane localization and conformation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/04e38e0553dd4095833d3e485d2fc850
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Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation

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