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

The response of titin to mechanical forces is a major determinant of the function of the heart. When placed under a pulling force, the unstructured regions of titin uncoil while its immunoglobulin (Ig) domains unfold and extend. Using single-molecule atomic force microscopy, we show that disulfide i...

Descripción completa

Detalles Bibliográficos
Autores principales: Giganti, David, Yan, Kevin, Badilla, Carmen L., Fernandez, Julio M., Alegre-Cebollada, Jorge
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5766482/
https://www.ncbi.nlm.nih.gov/pubmed/29330363
http://dx.doi.org/10.1038/s41467-017-02528-7

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5766482/
https://www.ncbi.nlm.nih.gov/pubmed/29330363
http://dx.doi.org/10.1038/s41467-017-02528-7

Ejemplares similares