Cargando…
Coupled molecular dynamics mediate long- and short-range epistasis between mutations that affect stability and aggregation kinetics
Multiple mutations are typically required to significantly improve protein stability or aggregation kinetics. However, when several substitutions are made in a single protein, the mutations can potentially interact in a nonadditive manner, resulting in epistatic effects, which can hamper protein-eng...
Autores principales: | Yu, Haoran, Dalby, Paul A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6255212/ https://www.ncbi.nlm.nih.gov/pubmed/30404916 http://dx.doi.org/10.1073/pnas.1810324115 |
Ejemplares similares
-
Exploiting correlated molecular-dynamics networks to counteract enzyme activity–stability trade-off
por: Yu, Haoran, et al.
Publicado: (2018) -
On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations
por: Yang, Xiaoting, et al.
Publicado: (2018) -
Predictive shifts in free energy couple mutations to their phenotypic consequences
por: Chure, Griffin, et al.
Publicado: (2019) -
Redox-coupled quinone dynamics in the respiratory complex I
por: Warnau, Judith, et al.
Publicado: (2018) -
Coupling between dynamic 3D tissue architecture and BMP morphogen signaling during Drosophila wing morphogenesis
por: Gui, Jinghua, et al.
Publicado: (2019)