The quasielastic neutron scattering index beta and the modulus of a protein's quasi-electric dipole moment were utilized to quantitate the thermostability of wildtype TC23O and its mutants. Charged residues Arg314, Glu246, Glu291, and some prolines near the C-terminus of the sequence (Pro228, Pro296, and Pro308) were identified to be critical for the thermostability of wildtype TC23O according to these two criteria. By analyzing the molecular conformation changes during the simulation, it was demonstrated how the mutant P228S was destabilized by disrupting two salt-bridges Asp116OD1-Lys215N and Glu210OE1-Lys217N at an adjacent beta-turn. The destabilization of P296S also shown to be intimate correlated with the break down of ion pair Lys188N-Glu291OE1. The sensitivity of its electrostatic network to the local structure is an important feature. It reveals that the 'proline effect' and electrostatic interactions together influences the thermostability of TC23O a lot.