Two-step self-assembly of a spider silk molecular clamp
Molecular details that underlie mechanical properties of spider silk are of great interest to material scientists. Here, the authors report a previously unknown three-state mechanism of folding and an expanded structure of a spider silk protein that may contribute to elasticity of spider silk.
Guardado en:
Autores principales: | Charlotte Rat, Julia C. Heiby, Jessica P. Bunz, Hannes Neuweiler |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/9eb7e6b4b3184de388ce25a4749dd5b3 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
por: Julia C. Heiby, et al.
Publicado: (2019) -
Composition and hierarchical organisation of a spider silk.
por: Alexander Sponner, et al.
Publicado: (2007) -
Tyrosine residues mediate supercontraction in biomimetic spider silk
por: Gabriele Greco, et al.
Publicado: (2021) -
Spider-silk inspired polymeric networks by harnessing the mechanical potential of β-sheets through network guided assembly
por: Nicholas Jun-An Chan, et al.
Publicado: (2020) -
Efficient protein production inspired by how spiders make silk
por: Nina Kronqvist, et al.
Publicado: (2017)