Acta Phys. -Chim. Sin. ›› 2002, Vol. 18 ›› Issue (08): 676-679.doi: 10.3866/PKU.WHXB20020802

• Communication • Previous Articles     Next Articles

New Method to Analyze Protein-protein Interaction Interface

Gao Ying;Wang Ren-Xiao;Lai Lu-Hua   

  1. State Key Laboratory of Structural Chemistry for Stable and Unstable Species, Institute of Physical Chemistry & College of Chemistry and Molecular Engineering, Peking University, Beijing 100871
  • Received:2002-04-03 Revised:2002-05-13 Published:2002-08-15
  • Contact: Lai Lu-Hua E-mail:lhlai@pku.edu.cn

Abstract: Hydrophobicity and hydrogen bonds are main factors governing protein-protein interaction. We have developed a new method, which only uses these two characteristics to figure the properties of protein-protein interface. With this method, we can easily pick out key residues at the interface and display this kind of characteristics using graphic software. This method has been applied to some examples and proved to be an useful tool for in-depth studies on protein-protein recognition.

Key words: Protein-protein interaction, PP_SITE procedure, Interface analysis, Correlated mutation