模型基于蛋白质表层的疏水残基 (hydrophobic residues)是蛋白质相互作用的主要因素这一生物学基础，在已有生 物学数据库的基础上，提出了蛋白质相互作用的MPK模型。
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These self-complementary peptides contain 50% charged amino acid residues, and are characterized by periodical repeats of alternating ionic hydrophilic and uncharged hydrophobic residuals.
这类自我互补的两亲寡肽含50%的带电残基，并且以交替的离子亲水性和不带电的氨基酸残基周期性重复为特征；
Moreover, the substituents on the bicyclic chromophore can also produce strong van der Waals and hydrophobic interactions with the residues located at the exterior part of the binding pocket.
同时，抑制剂双环上的取代基团也能和活性口袋外部的部分残基形成一定的范德华和疏水相互作用。
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