TY  - JOUR
TI  - Cation-π interactions in structural biology
AU  - Justin P. Gallivan
AU  - Dennis A. Dougherty
PY  - 1999
JO  - Proceedings of the National Academy of Sciences
DO  - 10.1073/pnas.96.17.9459
UR  - https://doi.org/10.1073/pnas.96.17.9459
AB  - Cation-pi interactions in protein structures are identified and evaluated by using an energy-based criterion for selecting significant sidechain pairs. Cation-pi 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-pi interaction. The sidechain of Arg is more likely than that of Lys to be in a cation-pi 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-pi interaction.
ER  -