The energy cost of polypeptide knot formation and its folding consequences

The effect of knots on protein stability and folding kinetics is not well understood. Here the authors combine optical tweezer experiments and calculations to experimentally determine the energy cost for knot formation, which indicates that knotted proteins evolved specific folding pathways because...

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Autores principales: Andrés Bustamante, Juan Sotelo-Campos, Daniel G. Guerra, Martin Floor, Christian A. M. Wilson, Carlos Bustamante, Mauricio Báez
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/3d303fa72ca546338630c764cd74af4c
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spelling oai:doaj.org-article:3d303fa72ca546338630c764cd74af4c2021-12-02T14:42:09ZThe energy cost of polypeptide knot formation and its folding consequences10.1038/s41467-017-01691-12041-1723https://doaj.org/article/3d303fa72ca546338630c764cd74af4c2017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01691-1https://doaj.org/toc/2041-1723The effect of knots on protein stability and folding kinetics is not well understood. Here the authors combine optical tweezer experiments and calculations to experimentally determine the energy cost for knot formation, which indicates that knotted proteins evolved specific folding pathways because knot formation in unfolded chains is unfavorable.Andrés BustamanteJuan Sotelo-CamposDaniel G. GuerraMartin FloorChristian A. M. WilsonCarlos BustamanteMauricio BáezNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Andrés Bustamante
Juan Sotelo-Campos
Daniel G. Guerra
Martin Floor
Christian A. M. Wilson
Carlos Bustamante
Mauricio Báez
The energy cost of polypeptide knot formation and its folding consequences
description The effect of knots on protein stability and folding kinetics is not well understood. Here the authors combine optical tweezer experiments and calculations to experimentally determine the energy cost for knot formation, which indicates that knotted proteins evolved specific folding pathways because knot formation in unfolded chains is unfavorable.
format article
author Andrés Bustamante
Juan Sotelo-Campos
Daniel G. Guerra
Martin Floor
Christian A. M. Wilson
Carlos Bustamante
Mauricio Báez
author_facet Andrés Bustamante
Juan Sotelo-Campos
Daniel G. Guerra
Martin Floor
Christian A. M. Wilson
Carlos Bustamante
Mauricio Báez
author_sort Andrés Bustamante
title The energy cost of polypeptide knot formation and its folding consequences
title_short The energy cost of polypeptide knot formation and its folding consequences
title_full The energy cost of polypeptide knot formation and its folding consequences
title_fullStr The energy cost of polypeptide knot formation and its folding consequences
title_full_unstemmed The energy cost of polypeptide knot formation and its folding consequences
title_sort energy cost of polypeptide knot formation and its folding consequences
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/3d303fa72ca546338630c764cd74af4c
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