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

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.

Bibliographic Details
Main Authors: Jörg Schönfelder, Raul Perez-Jimenez, Victor Muñoz
Format: Article
Language:English
Published: Nature Publishing Group 2016-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms11777
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spelling doaj-b0aaa035d8944396b1adbf1983ac4d332021-05-11T10:34:36ZengNature Publishing GroupNature Communications2041-17232016-06-01711810.1038/ncomms11777A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolutionJörg Schönfelder0Raul Perez-Jimenez1Victor Muñoz2Department of Macromolecular Structures, National Biotechnology Center, Consejo Superior de Investigaciones CientíficasNanobiomechanics Laboratory, CIC nanoGUNEDepartment of Macromolecular Structures, National Biotechnology Center, Consejo Superior de Investigaciones CientíficasPrevious 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.https://doi.org/10.1038/ncomms11777
collection DOAJ
language English
format Article
sources DOAJ
author Jörg Schönfelder
Raul Perez-Jimenez
Victor Muñoz
spellingShingle Jörg Schönfelder
Raul Perez-Jimenez
Victor Muñoz
A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2016-06-01
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.
url https://doi.org/10.1038/ncomms11777
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AT victormunoz asimpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
AT jorgschonfelder simpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
AT raulperezjimenez simpletwostateproteinunfoldsmechanicallyviamultipleheterogeneouspathwaysatsinglemoleculeresolution
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