EFFECTS OF ELECTROSTATIC AND HYDROPHOBIC INTERACTIONON THE STABILITY OF INSULIN DIMER
静电和疏水效应对胰岛素二聚体稳定性的影响

The crystal structure of the pig insulin dimer (4ins) was used to study the electrostatic and hydrophobic interactions between two monomers. The Continuum model and the finite difference Poisson-Boltzmann (FDPB) method were used to calculate the electrostatic potentials of the system. The molecular surface was explored in the condition of different pH values. The results indicate that the electrostatic interaction energy and the desolvation free energy show smaller values when pH values are between 4.6 and 8.5. The hydrophobicity denotes an obvious peak when pH is near 6.2. These results are consistent with the experimental condition for insulin dimer crystallization.