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

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...

Full description

Bibliographic Details
Main Authors: Peng Xiao, David Bolton, Rachel A. Munro, Leonid S. Brown, Vladimir Ladizhansky
Format: Article
Language:English
Published: Nature Publishing Group 2019-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-11849-8
id doaj-598def11c2fc4bcd97e663bc018acd2a
record_format Article
spelling doaj-598def11c2fc4bcd97e663bc018acd2a2021-05-11T11:54:41ZengNature Publishing GroupNature Communications2041-17232019-08-0110111110.1038/s41467-019-11849-8Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathwayPeng Xiao0David Bolton1Rachel A. Munro2Leonid S. Brown3Vladimir Ladizhansky4Department of Physics and Biophysics Interdepartmental Group, University of GuelphDepartment of Physics and Biophysics Interdepartmental Group, University of GuelphDepartment of Physics and Biophysics Interdepartmental Group, University of GuelphDepartment of Physics and Biophysics Interdepartmental Group, University of GuelphDepartment of Physics and Biophysics Interdepartmental Group, University of GuelphStudying 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.https://doi.org/10.1038/s41467-019-11849-8
collection DOAJ
language English
format Article
sources DOAJ
author Peng Xiao
David Bolton
Rachel A. Munro
Leonid S. Brown
Vladimir Ladizhansky
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-08-01
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.
url https://doi.org/10.1038/s41467-019-11849-8
work_keys_str_mv AT pengxiao solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway
AT davidbolton solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway
AT rachelamunro solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway
AT leonidsbrown solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway
AT vladimirladizhansky solidstatenmrspectroscopybasedatomisticviewofamembraneproteinunfoldingpathway
_version_ 1721445727495782400

Similar Items