Chemical unfolding of protein domains induces shape change in programmed protein hydrogels
Tailoring and programing the behavior of protein biomaterials is complex. Here, the authors report on the use of polyelectrolytes for controlling the stiffness to allow programing of protein hydrogels and generate reversible shape changes via folding and unfolding reactions.
Guardado en:
Autores principales: | Luai R. Khoury, Ionel Popa |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/1b58a0cca96746848ac2a2cc3027d7d4 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.
por: Shashi Kumar Suman, et al.
Publicado: (2013) -
Hypoxia-induced SETX links replication stress with the unfolded protein response
por: Shaliny Ramachandran, et al.
Publicado: (2021) -
Periplocin and cardiac glycosides suppress the unfolded protein response
por: Muneshige Tokugawa, et al.
Publicado: (2021) -
The physiological role of the unfolded protein response in plants
por: Moreno,Adrian A, et al.
Publicado: (2011) -
Protein context shapes the specificity of SH3 domain-mediated interactions in vivo
por: Ugo Dionne, et al.
Publicado: (2021)