Correlation of membrane protein conformational and functional dynamics

High-speed atomic force microscopy height spectroscopy and single channel electrophysiology recordings are used to correlate conformational and functional dynamics of the model membrane protein, outer membrane protein G (OmpG). These techniques show that both states coexist and rapidly interchange i...

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Autores principales:	Raghavendar Reddy Sanganna Gari, Joel José Montalvo‐Acosta, George R. Heath, Yining Jiang, Xiaolong Gao, Crina M. Nimigean, Christophe Chipot, Simon Scheuring
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/244843fefff4420181bab8bb8e548a7e
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spelling	oai:doaj.org-article:244843fefff4420181bab8bb8e548a7e2021-12-02T17:01:21ZCorrelation of membrane protein conformational and functional dynamics10.1038/s41467-021-24660-12041-1723https://doaj.org/article/244843fefff4420181bab8bb8e548a7e2021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24660-1https://doaj.org/toc/2041-1723High-speed atomic force microscopy height spectroscopy and single channel electrophysiology recordings are used to correlate conformational and functional dynamics of the model membrane protein, outer membrane protein G (OmpG). These techniques show that both states coexist and rapidly interchange in all conditions supported by molecular dynamics simulations.Raghavendar Reddy Sanganna GariJoel José Montalvo‐AcostaGeorge R. HeathYining JiangXiaolong GaoCrina M. NimigeanChristophe ChipotSimon ScheuringNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Raghavendar Reddy Sanganna Gari Joel José Montalvo‐Acosta George R. Heath Yining Jiang Xiaolong Gao Crina M. Nimigean Christophe Chipot Simon Scheuring Correlation of membrane protein conformational and functional dynamics
description	High-speed atomic force microscopy height spectroscopy and single channel electrophysiology recordings are used to correlate conformational and functional dynamics of the model membrane protein, outer membrane protein G (OmpG). These techniques show that both states coexist and rapidly interchange in all conditions supported by molecular dynamics simulations.
format	article
author	Raghavendar Reddy Sanganna Gari Joel José Montalvo‐Acosta George R. Heath Yining Jiang Xiaolong Gao Crina M. Nimigean Christophe Chipot Simon Scheuring
author_facet	Raghavendar Reddy Sanganna Gari Joel José Montalvo‐Acosta George R. Heath Yining Jiang Xiaolong Gao Crina M. Nimigean Christophe Chipot Simon Scheuring
author_sort	Raghavendar Reddy Sanganna Gari
title	Correlation of membrane protein conformational and functional dynamics
title_short	Correlation of membrane protein conformational and functional dynamics
title_full	Correlation of membrane protein conformational and functional dynamics
title_fullStr	Correlation of membrane protein conformational and functional dynamics
title_full_unstemmed	Correlation of membrane protein conformational and functional dynamics
title_sort	correlation of membrane protein conformational and functional dynamics
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/244843fefff4420181bab8bb8e548a7e
work_keys_str_mv	AT raghavendarreddysangannagari correlationofmembraneproteinconformationalandfunctionaldynamics AT joeljosemontalvoacosta correlationofmembraneproteinconformationalandfunctionaldynamics AT georgerheath correlationofmembraneproteinconformationalandfunctionaldynamics AT yiningjiang correlationofmembraneproteinconformationalandfunctionaldynamics AT xiaolonggao correlationofmembraneproteinconformationalandfunctionaldynamics AT crinamnimigean correlationofmembraneproteinconformationalandfunctionaldynamics AT christophechipot correlationofmembraneproteinconformationalandfunctionaldynamics AT simonscheuring correlationofmembraneproteinconformationalandfunctionaldynamics
_version_	1718382134362636288

Correlation of membrane protein conformational and functional dynamics

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