Improvement of Thermal Stability of DFPase by In silico Methods

Efficiency of enzymes which are used in industrial or environmental applications is highly dependent on their thermal stability. In this study, the stability of DFPasehas been evaluated after introducing disulfide bonds to the structure. The results obtained from a series of protein design software were subjected to moleculardynamics simulation at different temperature to test the performance of such combinatorial procedure. Amount several designs, mutation M5 showed desirablethermostability via molecular dynamics simulation and normal mode analysis. As it clearly depicted, such in silico structural investigations would be resulted in reducing the numerous choices of experimental options as it was undergone a series of computational evaluation previously.

Keywords:

Rational Design , DFPase , Enzyme Stability , Molecular Dynamics Simulation , Normal Mode Analysis