Ultrahigh specificity in a network of computationally designed protein-interaction pairs
The molecular basis of ultrahigh specificity in protein-protein interactions remains obscure. The authors present a computational method to design atomically accurate new pairs exhibiting >100,000-fold specificity switches, generating a large and complex interaction network.
Guardado en:
Autores principales: | Ravit Netzer, Dina Listov, Rosalie Lipsh, Orly Dym, Shira Albeck, Orli Knop, Colin Kleanthous, Sarel J. Fleishman |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/9939e24b02bd4d13a295f4878802d25a |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Highly active enzymes by automated combinatorial backbone assembly and sequence design
por: Gideon Lapidoth, et al.
Publicado: (2018) -
Ultrahigh-Throughput Multiplexing and Sequencing of >500-Base-Pair Amplicon Regions on the Illumina HiSeq 2500 Platform
por: Johanna B. Holm, et al.
Publicado: (2019) -
Interpenetration of polymeric microgels at ultrahigh densities
por: Priti S. Mohanty, et al.
Publicado: (2017) -
On-chip terahertz isolator with ultrahigh isolation ratios
por: Shixing Yuan, et al.
Publicado: (2021) -
Computational stabilization of T cell receptors allows pairing with antibodies to form bispecifics
por: Karen Froning, et al.
Publicado: (2020)