Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity

Titin regulates myocyte stiffness through uncoiling and unfolding but these two processes cannot fully explain its elasticity. Here, the authors use atomic force microscopy to study the properties of titin disulfide bonds, showing that disulfide isomerization represents a third mode of titin elastic...

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Autores principales:	David Giganti, Kevin Yan, Carmen L. Badilla, Julio M. Fernandez, Jorge Alegre-Cebollada
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/bb0d9fa1d8914904b64c583908b5ecca
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spelling	oai:doaj.org-article:bb0d9fa1d8914904b64c583908b5ecca2021-12-02T16:50:11ZDisulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity10.1038/s41467-017-02528-72041-1723https://doaj.org/article/bb0d9fa1d8914904b64c583908b5ecca2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02528-7https://doaj.org/toc/2041-1723Titin regulates myocyte stiffness through uncoiling and unfolding but these two processes cannot fully explain its elasticity. Here, the authors use atomic force microscopy to study the properties of titin disulfide bonds, showing that disulfide isomerization represents a third mode of titin elasticity.David GigantiKevin YanCarmen L. BadillaJulio M. FernandezJorge Alegre-CebolladaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q David Giganti Kevin Yan Carmen L. Badilla Julio M. Fernandez Jorge Alegre-Cebollada Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
description	Titin regulates myocyte stiffness through uncoiling and unfolding but these two processes cannot fully explain its elasticity. Here, the authors use atomic force microscopy to study the properties of titin disulfide bonds, showing that disulfide isomerization represents a third mode of titin elasticity.
format	article
author	David Giganti Kevin Yan Carmen L. Badilla Julio M. Fernandez Jorge Alegre-Cebollada
author_facet	David Giganti Kevin Yan Carmen L. Badilla Julio M. Fernandez Jorge Alegre-Cebollada
author_sort	David Giganti
title	Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
title_short	Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
title_full	Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
title_fullStr	Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
title_full_unstemmed	Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
title_sort	disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/bb0d9fa1d8914904b64c583908b5ecca
work_keys_str_mv	AT davidgiganti disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity AT kevinyan disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity AT carmenlbadilla disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity AT juliomfernandez disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity AT jorgealegrecebollada disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity
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Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity

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