物理化学学报 >> 2002, Vol. 18 >> Issue (08): 676-679.doi: 10.3866/PKU.WHXB20020802

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分析蛋白质-蛋白质相互作用界面的新方法

高莹;王任小;来鲁华   

  1. 北京大学化学与分子工程学院物理化学研究所，分子动态与稳态结构国家重点实验室，北京　100871
  • 收稿日期:2002-04-03 修回日期:2002-05-13 发布日期:2002-08-15
  • 通讯作者: 来鲁华 E-mail:lhlai@pku.edu.cn

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

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摘要： 疏水性和氢键是蛋白质-蛋白质相互作用中的主要因素.提出一种新的计算方法，从蛋白受体的结合部位推导出蛋白配体相应部位应该具有的疏水性质和氢键性质.应用这种方法可以很容易地找出影响相互作用的关键残基，并且将界面的这两种特征用图形软件显示出来.在应用到实际蛋白-蛋白相互作用中时，发现它的用途并不限于此.它可以作为研究蛋白相互作用的一个基本工具.

关键词: 蛋白质-蛋白质相互作用, PP_SITE程序, 界面分析, 相关突变

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