阳离子聚合
蛋白质数据库
化学
圆周率
结晶学
蛋白质结构
立体化学
生物化学
有机化学
作者
Justin P. Gallivan,Dennis A. Dougherty
标识
DOI:10.1073/pnas.96.17.9459
摘要
Cation-π interactions in protein structures are identified and evaluated by using an energy-based criterion for selecting significant sidechain pairs. Cation-π interactions are found to be common among structures in the Protein Data Bank, and it is clearly demonstrated that, when a cationic sidechain (Lys or Arg) is near an aromatic sidechain (Phe, Tyr, or Trp), the geometry is biased toward one that would experience a favorable cation-π interaction. The sidechain of Arg is more likely than that of Lys to be in a cation-π interaction. Among the aromatics, a strong bias toward Trp is clear, such that over one-fourth of all tryptophans in the data bank experience an energetically significant cation-π interaction.
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