Article
A strategy based on thermal flexibility to design triosephosphate isomerase proteins with increased or decreased kinetic stability.
Biochemical and biophysical research communications - 18 Sept 2018
Quezada Andrea G, Cabrera Nallely, Piñeiro Ángel, Díaz-Salazar A Jessica, Díaz-Mazariegos Selma, Romero-Romero Sergio, Pérez-Montfort Ruy, Costas Miguel
Abstract excerpt
Kinetic stability of proteins determines their susceptibility to irreversibly unfold in a time-dependent process, and therefore its half-life. A residue displacement analysis of temperature-induced unfolding molecular dynamics simulations was recently employed to define the thermal flexibility of proteins. This property was found to be correlated with the activation energy barrier (Eact) separating the native...
Topics
- Enzyme Stability
- Kinetics
- Models, Molecular
- Mutation
- Protein Denaturation
- Protein Engineering
- Protein Unfolding
- Temperature
- Triose-Phosphate Isomerase
- Trypanosoma brucei brucei