title: Thermostability of protein studied by molecular dynamics simulation.
abstract: The thermostability of protein thermostable cathechol 2,3-dixoygenase (TC23O) has been studied by the parallel molecular dynamics simulations. By analysis of the exponent beta, which is related to the scattering spectrum and constant-pressure heat capacity Cp, we reveal the respective contribution of a specific residue 228 proline; a specific salt bridge, Lys188N-Glu291OE1; four ions; and a different water environment to the thermostability of TC23O. The dynamic transition temperature of the mutants, Pro228Ser and Glu291Gly of the TC23O, was decreased about 10 degrees C and 19 degrees C respectively. The displacement of the four ions had no significant effect on the thermostability of TC23O. Water affects the thermostability by influencing the changes of accessible conformation to a certain extent. All these results agree with the known experimental results.
authors.affiliation: Surface Physics Key Laboratory Department of Physics, Fudan University, China.
authors.forename: Jian-Hua
authors.initials: JH
authors.lastname: Zhang
authors.forename: Li-Li
authors.initials: LL
authors.lastname: Zhang
authors.forename: Lin-Xiang
authors.initials: LX
authors.lastname: Zhou
mesh_terms: D050557:Catechol 2,3-Dioxygenase; D003627:Data Interpretation, Statistical; D049308:Dioxygenases; D006358:Hot Temperature; D007700:Kinetics; D008958:Models, Molecular; D010105:Oxygenases / Q000737:chemistry*
chemical_list: D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase