Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins
Further improvement of the thermostability of inherently thermostable proteins is an attractive challenge because more thermostable proteins are industrially more useful and serve as better scaffolds for protein engineering. To establish guidelines that can be applied for the rational design of hype...
Guardado en:
Autores principales: | Satoshi Akanuma, Minako Yamaguchi, Akihiko Yamagishi |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/8fdae7d8638943b3a90e546a4958bcbd |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins.
por: Satoshi Akanuma, et al.
Publicado: (2021) -
Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability
por: Xiutao Chen, et al.
Publicado: (2018) -
Comprehensive reduction of amino acid set in a protein suggests the importance of prebiotic amino acids for stable proteins
por: Rei Shibue, et al.
Publicado: (2018) -
Enzyme activity and thermostability of a non-specific nuclease from Yersinia enterocolitica subsp. palearctica by site-directed mutagenesis
por: Zhang,Yu, et al.
Publicado: (2016) -
Thermostable exoshells fold and stabilize recombinant proteins
por: Siddharth Deshpande, et al.
Publicado: (2017)