Protein unfolding as a switch from self-recognition to high-affinity client binding

Under stress conditions the molecular chaperone Hsp33 is activated to process unfolded proteins. Here, the authors use in vivo and in vitro crosslinking and 19F-NMR to elucidate the binding site for misfolded proteins and are able to propose a model for its mechanism of action.

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Autores principales:	Bastian Groitl, Scott Horowitz, Karl A. T. Makepeace, Evgeniy V. Petrotchenko, Christoph H. Borchers, Dana Reichmann, James C. A. Bardwell, Ursula Jakob
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/695b2905d3a942f196334c70c8cf5b8c
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spelling	oai:doaj.org-article:695b2905d3a942f196334c70c8cf5b8c2021-12-02T14:39:54ZProtein unfolding as a switch from self-recognition to high-affinity client binding10.1038/ncomms103572041-1723https://doaj.org/article/695b2905d3a942f196334c70c8cf5b8c2016-01-01T00:00:00Zhttps://doi.org/10.1038/ncomms10357https://doaj.org/toc/2041-1723Under stress conditions the molecular chaperone Hsp33 is activated to process unfolded proteins. Here, the authors use in vivo and in vitro crosslinking and 19F-NMR to elucidate the binding site for misfolded proteins and are able to propose a model for its mechanism of action.Bastian GroitlScott HorowitzKarl A. T. MakepeaceEvgeniy V. PetrotchenkoChristoph H. BorchersDana ReichmannJames C. A. BardwellUrsula JakobNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Bastian Groitl Scott Horowitz Karl A. T. Makepeace Evgeniy V. Petrotchenko Christoph H. Borchers Dana Reichmann James C. A. Bardwell Ursula Jakob Protein unfolding as a switch from self-recognition to high-affinity client binding
description	Under stress conditions the molecular chaperone Hsp33 is activated to process unfolded proteins. Here, the authors use in vivo and in vitro crosslinking and 19F-NMR to elucidate the binding site for misfolded proteins and are able to propose a model for its mechanism of action.
format	article
author	Bastian Groitl Scott Horowitz Karl A. T. Makepeace Evgeniy V. Petrotchenko Christoph H. Borchers Dana Reichmann James C. A. Bardwell Ursula Jakob
author_facet	Bastian Groitl Scott Horowitz Karl A. T. Makepeace Evgeniy V. Petrotchenko Christoph H. Borchers Dana Reichmann James C. A. Bardwell Ursula Jakob
author_sort	Bastian Groitl
title	Protein unfolding as a switch from self-recognition to high-affinity client binding
title_short	Protein unfolding as a switch from self-recognition to high-affinity client binding
title_full	Protein unfolding as a switch from self-recognition to high-affinity client binding
title_fullStr	Protein unfolding as a switch from self-recognition to high-affinity client binding
title_full_unstemmed	Protein unfolding as a switch from self-recognition to high-affinity client binding
title_sort	protein unfolding as a switch from self-recognition to high-affinity client binding
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/695b2905d3a942f196334c70c8cf5b8c
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Protein unfolding as a switch from self-recognition to high-affinity client binding

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