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

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...

Full description

Bibliographic Details
Main Authors: David Giganti, Kevin Yan, Carmen L. Badilla, Julio M. Fernandez, Jorge Alegre-Cebollada
Format: Article
Language:English
Published: Nature Publishing Group 2018-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02528-7
id doaj-bb0d9fa1d8914904b64c583908b5ecca
record_format Article
spelling doaj-bb0d9fa1d8914904b64c583908b5ecca2021-05-11T10:15:40ZengNature Publishing GroupNature Communications2041-17232018-01-019111110.1038/s41467-017-02528-7Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticityDavid Giganti0Kevin Yan1Carmen L. Badilla2Julio M. Fernandez3Jorge Alegre-Cebollada4Department of Biological Sciences, Columbia UniversityDepartment of Biological Sciences, Columbia UniversityDepartment of Biological Sciences, Columbia UniversityDepartment of Biological Sciences, Columbia UniversityCentro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC)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.https://doi.org/10.1038/s41467-017-02528-7
collection DOAJ
language English
format Article
sources DOAJ
author David Giganti
Kevin Yan
Carmen L. Badilla
Julio M. Fernandez
Jorge Alegre-Cebollada
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-01-01
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.
url https://doi.org/10.1038/s41467-017-02528-7
work_keys_str_mv AT davidgiganti disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity
AT kevinyan disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity
AT carmenlbadilla disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity
AT juliomfernandez disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity
AT jorgealegrecebollada disulfideisomerizationreactionsintitinimmunoglobulindomainsenableamodeofproteinelasticity
_version_ 1721448544901005312

Similar Items