Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes

The intrinsically disordered linker histone H1.0 and prothymosin α form a complex which exhibits slow exchange between bound and unbound populations at low protein concentrations and fast exchange at high concentrations. Here authors explain this observation by the formation of transient ternary com...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Andrea Sottini, Alessandro Borgia, Madeleine B. Borgia, Katrine Bugge, Daniel Nettels, Aritra Chowdhury, Pétur O. Heidarsson, Franziska Zosel, Robert B. Best, Birthe B. Kragelund, Benjamin Schuler
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/64b405d60211411596d26e2756ae1e36
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:64b405d60211411596d26e2756ae1e36
record_format	dspace
spelling	oai:doaj.org-article:64b405d60211411596d26e2756ae1e362021-12-02T14:42:50ZPolyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes10.1038/s41467-020-18859-x2041-1723https://doaj.org/article/64b405d60211411596d26e2756ae1e362020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18859-xhttps://doaj.org/toc/2041-1723The intrinsically disordered linker histone H1.0 and prothymosin α form a complex which exhibits slow exchange between bound and unbound populations at low protein concentrations and fast exchange at high concentrations. Here authors explain this observation by the formation of transient ternary complexes favored at high protein concentrations that accelerate the exchange.Andrea SottiniAlessandro BorgiaMadeleine B. BorgiaKatrine BuggeDaniel NettelsAritra ChowdhuryPétur O. HeidarssonFranziska ZoselRobert B. BestBirthe B. KragelundBenjamin SchulerNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Andrea Sottini Alessandro Borgia Madeleine B. Borgia Katrine Bugge Daniel Nettels Aritra Chowdhury Pétur O. Heidarsson Franziska Zosel Robert B. Best Birthe B. Kragelund Benjamin Schuler Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
description	The intrinsically disordered linker histone H1.0 and prothymosin α form a complex which exhibits slow exchange between bound and unbound populations at low protein concentrations and fast exchange at high concentrations. Here authors explain this observation by the formation of transient ternary complexes favored at high protein concentrations that accelerate the exchange.
format	article
author	Andrea Sottini Alessandro Borgia Madeleine B. Borgia Katrine Bugge Daniel Nettels Aritra Chowdhury Pétur O. Heidarsson Franziska Zosel Robert B. Best Birthe B. Kragelund Benjamin Schuler
author_facet	Andrea Sottini Alessandro Borgia Madeleine B. Borgia Katrine Bugge Daniel Nettels Aritra Chowdhury Pétur O. Heidarsson Franziska Zosel Robert B. Best Birthe B. Kragelund Benjamin Schuler
author_sort	Andrea Sottini
title	Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
title_short	Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
title_full	Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
title_fullStr	Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
title_full_unstemmed	Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
title_sort	polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/64b405d60211411596d26e2756ae1e36
work_keys_str_mv	AT andreasottini polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT alessandroborgia polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT madeleinebborgia polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT katrinebugge polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT danielnettels polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT aritrachowdhury polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT peturoheidarsson polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT franziskazosel polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT robertbbest polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT birthebkragelund polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes AT benjaminschuler polyelectrolyteinteractionsenablerapidassociationanddissociationinhighaffinitydisorderedproteincomplexes
_version_	1718389573061443584

Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes

Ejemplares similares