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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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
Description
Summary: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.
ISSN:2041-1723