TY - JOUR ID - 69155 TI - Improvement of Thermal Stability of DFPase by In silico Methods JO - Journal of Applied Biotechnology Reports JA - JABR LA - en SN - 2322-1186 AU - Mirzaei, Morteza AU - Latifi, Ali Mohammad AU - Jafari, Rahim AD - Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran AD - Department of Nanobiotechnology, Faculty of Bio-logical Sciences, Tarbiat Modares University, Tehran, Iran Y1 - 2014 PY - 2014 VL - 1 IS - 4 SP - 155 EP - 159 KW - Rational Design KW - DFPase KW - Enzyme Stability KW - Molecular Dynamics Simulation KW - Nor-mal Mode Analysis DO - N2 - 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. UR - https://www.biotechrep.ir/article_69155.html L1 - https://www.biotechrep.ir/article_69155_f4f067167149bdb2635284d762b68900.pdf ER -