A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution

Previous investigations have indicated that the model protein CspB folds in a simple two-state fashion. Here, the authors provide direct experimental evidence for that the energy landscape of two-state folding proteins is highly heterogeneous and that unfolding can occur via multiple pathways.

Guardado en:
Detalles Bibliográficos
Autores principales: Jörg Schönfelder, Raul Perez-Jimenez, Victor Muñoz
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
Materias:
Q
Acceso en línea:https://doaj.org/article/b0aaa035d8944396b1adbf1983ac4d33
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:b0aaa035d8944396b1adbf1983ac4d33
record_format dspace
spelling oai:doaj.org-article:b0aaa035d8944396b1adbf1983ac4d332021-12-02T16:56:44ZA simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution10.1038/ncomms117772041-1723https://doaj.org/article/b0aaa035d8944396b1adbf1983ac4d332016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms11777https://doaj.org/toc/2041-1723Previous investigations have indicated that the model protein CspB folds in a simple two-state fashion. Here, the authors provide direct experimental evidence for that the energy landscape of two-state folding proteins is highly heterogeneous and that unfolding can occur via multiple pathways.Jörg SchönfelderRaul Perez-JimenezVictor MuñozNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jörg Schönfelder
Raul Perez-Jimenez
Victor Muñoz
A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
description Previous investigations have indicated that the model protein CspB folds in a simple two-state fashion. Here, the authors provide direct experimental evidence for that the energy landscape of two-state folding proteins is highly heterogeneous and that unfolding can occur via multiple pathways.
format article
author Jörg Schönfelder
Raul Perez-Jimenez
Victor Muñoz
author_facet Jörg Schönfelder
Raul Perez-Jimenez
Victor Muñoz
author_sort Jörg Schönfelder
title A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
title_short A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
title_full A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
title_fullStr A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
title_full_unstemmed A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
title_sort simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/b0aaa035d8944396b1adbf1983ac4d33
work_keys_str_mv AT jorgschonfelder asimpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
AT raulperezjimenez asimpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
AT victormunoz asimpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
AT jorgschonfelder simpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
AT raulperezjimenez simpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
AT victormunoz simpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
_version_ 1718382762042327040