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...
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 |
Similar Items
-
Redox regulation of protein nanomechanics in health and disease: Lessons from titin
by: Elías Herrero-Galán, et al.
Published: (2019-02-01) -
Roles of Titin in the Structure and Elasticity of the Sarcomere
by: Larissa Tskhovrebova, et al.
Published: (2010-01-01) -
Mechanical network in titin immunoglobulin from force distribution analysis.
by: Wolfram Stacklies, et al.
Published: (2009-03-01) -
Studies on the polarity and functional domains of the titin molecule
by: Sun, Mu-Chien, et al.
Published: (1991) -
Titin role in muscle homeostasis : the kinase domain
by: Bogomolovas, Julijus
Published: (2014)