Acta Phys. -Chim. Sin. ›› 2004, Vol. 20 ›› Issue (06): 587-592.doi: 10.3866/PKU.WHXB20040607

• ARTICLE • Previous Articles     Next Articles

Efffects of Electrostatic and Hydrophobic Interaction on the Stability of the TGEV Main Proteinase Dimer

Zheng Ke-Wen;Yu Qing-Sen;Zeng Min;Ma Guo-Zheng;Wang Yan-Hua;Zhang Bing   

  1. Department of Chemistry, Zhejiang University, Hangzhou 310027;Key Laboratory for Molecular Design and Nutrition Engineering of Ningbo City, Ningbo Institute of Technology, Zhejiang University, Ningbo 315100
  • Received:2003-11-11 Revised:2004-02-17 Published:2004-06-15
  • Contact: Zeng Min

Abstract: The crystal structures of the TGEV 3CL proteinase is used to study the electrostatic and hydrophobic interactions between two monomers. Solving the Poisson-Boltzmanne equation using the finite difference method is used to calculate the electrostatic potential. The solvent accessible surface model is supplied for the molecular surface and hydrophobicity. The electrostatic and hydrophobic interactions are explored in the condition of different pH values. The electrostatic interaction energy, electrostatic desolvation free energy, and hydrophobic desolvation free energy show smaller values when pH values are between 5.5 and 8.5, which indicates that, in the condition, the electrostatic and hydrophobic interaction are favorable to the stability of the TGEV 3CL proteinase dimer. The results are consistent with the experimental condition for the crystallization of the TGEV 3CL proteinase dimer. pH values have stronger influence on the electrostatic desolvation free energy than on the hydrophobic desolvation free energy, which implies that the electrostatic interaction is the key factor to the instability of the TGEV 3Cl proteinase dimer in acid or alkali condition.

Key words: TGEV(transmissible gastroenteritis virus of swine) 3CL proteinase dimer, Electrostatic interaction, Hydrophobic effects, pH value