Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst.

Computational design of protein catalysts with enhanced stabilities for use in research and enzyme technologies is a challenging task. Using force-field calculations and phylogenetic analysis, we previously designed the haloalkane dehalogenase DhaA115 which contains 11 mutations that confer upon it outstanding thermostability ( = 73.5 °C; Δ > 23 °C).