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...
Enregistré dans:
Auteurs principaux: | David Giganti, Kevin Yan, Carmen L. Badilla, Julio M. Fernandez, Jorge Alegre-Cebollada |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2018
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/bb0d9fa1d8914904b64c583908b5ecca |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Mechanical network in titin immunoglobulin from force distribution analysis.
par: Wolfram Stacklies, et autres
Publié: (2009) -
Directing isomerization reactions of cumulenes with electric fields
par: Yaping Zang, et autres
Publié: (2019) -
Overcoming the thermodynamic equilibrium of an isomerization reaction through oxidoreductive reactions for biotransformation
par: Jing-Jing Liu, et autres
Publié: (2019) -
Selective E to Z isomerization of 1,3-Dienes Enabled by A Dinuclear Mechanism
par: Eiji Kudo, et autres
Publié: (2021) -
The giant protein titin regulates the length of the striated muscle thick filament
par: Paola Tonino, et autres
Publié: (2017)