Protein folding while chaperone bound is dependent on weak interactions

Spy is an ATP independent chaperone that allows folding of its client protein Im7 while continuously bound to Spy. Here the authors employ kinetics measurements to study the folding of another Spy client protein SH3 and find that Spy’s ability to allow a client to fold while bound is inversely relat...

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Autores principales:	Kevin Wu, Frederick Stull, Changhan Lee, James C. A. Bardwell
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8c86c6c179904e2d898f9faec9e90757
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spelling	oai:doaj.org-article:8c86c6c179904e2d898f9faec9e907572021-12-02T16:57:40ZProtein folding while chaperone bound is dependent on weak interactions10.1038/s41467-019-12774-62041-1723https://doaj.org/article/8c86c6c179904e2d898f9faec9e907572019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12774-6https://doaj.org/toc/2041-1723Spy is an ATP independent chaperone that allows folding of its client protein Im7 while continuously bound to Spy. Here the authors employ kinetics measurements to study the folding of another Spy client protein SH3 and find that Spy’s ability to allow a client to fold while bound is inversely related to how strongly it interacts with that client.Kevin WuFrederick StullChanghan LeeJames C. A. BardwellNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kevin Wu Frederick Stull Changhan Lee James C. A. Bardwell Protein folding while chaperone bound is dependent on weak interactions
description	Spy is an ATP independent chaperone that allows folding of its client protein Im7 while continuously bound to Spy. Here the authors employ kinetics measurements to study the folding of another Spy client protein SH3 and find that Spy’s ability to allow a client to fold while bound is inversely related to how strongly it interacts with that client.
format	article
author	Kevin Wu Frederick Stull Changhan Lee James C. A. Bardwell
author_facet	Kevin Wu Frederick Stull Changhan Lee James C. A. Bardwell
author_sort	Kevin Wu
title	Protein folding while chaperone bound is dependent on weak interactions
title_short	Protein folding while chaperone bound is dependent on weak interactions
title_full	Protein folding while chaperone bound is dependent on weak interactions
title_fullStr	Protein folding while chaperone bound is dependent on weak interactions
title_full_unstemmed	Protein folding while chaperone bound is dependent on weak interactions
title_sort	protein folding while chaperone bound is dependent on weak interactions
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/8c86c6c179904e2d898f9faec9e90757
work_keys_str_mv	AT kevinwu proteinfoldingwhilechaperoneboundisdependentonweakinteractions AT frederickstull proteinfoldingwhilechaperoneboundisdependentonweakinteractions AT changhanlee proteinfoldingwhilechaperoneboundisdependentonweakinteractions AT jamescabardwell proteinfoldingwhilechaperoneboundisdependentonweakinteractions
_version_	1718382512645865472

Protein folding while chaperone bound is dependent on weak interactions

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