Abstract

Efficiency of enzymes which are used in industrial or environmental applications is highly dependent on their thermal stability. In this study, the stability of DFPase has been evaluated after introducing disulfide bonds to the structure. The results obtained from a series of protein design software were subjected to molecular dynamics simulation at different temperature to test the performance of such combinatorial procedure. Amount several designs, mutation M5 showed desirable thermostability 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. © 2014, Baqiyatallah university of medical sciences. All rights reserved.