Cation–pi interaction in protein structures（1）

In addition to noncovalent interactions, the cation-π interaction (Dougherty, 1996) is recognized as an important noncovalent binding interaction relevant to structural biology. It is formed by the interaction of the positively charged residues, Lys and Arg, with the aromatic residues, Phe, Trp, and Tyr. Gallivan and Dougherty (1999) identified and evaluated cation-π interactions in protein structures. They reported that cation-π interactions are commonly occurring in protein structures in such a way that when a cationic side chain (Lys or Arg) is near to an aromatic side chain (Phe, Tyr, or Trp), the geometry is biased toward one that would experience a favorable cation-π interaction.
阳离子-π相互作用（Dougherty，1996）被认为是与结构生物学相关的重要的非共价结合相互作用。它由带正电的残基Lys和Arg与芳香族残基Phe，Trp和Tyr相互作用而形成。 Gallivan和Dougherty（1999）发现和评估了蛋白质结构中的阳离子-π相互作用。他们报道，阳离子-π相互作用通常以这样的方式发生在蛋白质结构中，当阳离子侧链（Lys或Arg）靠近芳香侧链（Phe，Tyr或Trp）