Burley S K, Petsko G A
FEBS Lett. 1986 Jul 28;203(2):139-43. doi: 10.1016/0014-5793(86)80730-x.
Geometric analysis of 33 refined high-resolution protein crystal structures (2 A or higher) demonstrates that side-chain amino groups interact with aromatic side chains. Positively charged or delta(+) amino groups of lysine, arginine, asparagine, glutamine and histidine are preferentially located within 6 A of the ring centroids of phenylalanine, tyrosine and tryptophan, where they make van der Waals' contact with the delta(-) pi-electrons and avoid the delta(+) ring edge. This geometric pattern is different from the distribution expected due to random close packing of side chains in a protein. It is opposite to oxygen- and sulfur-aromatic interactions, similar to aromatic-aromatic interactions, and almost certainly electrostatic in origin.
对33个精制的高分辨率蛋白质晶体结构（2埃或更高）进行几何分析表明，侧链氨基与芳香族侧链相互作用。赖氨酸、精氨酸、天冬酰胺、谷氨酰胺和组氨酸的带正电荷或δ（+）氨基优先位于苯丙氨酸、酪氨酸和色氨酸环质心的6埃范围内，在那里它们与δ（-）π电子形成范德华接触，并避开δ（+）环边缘。这种几何模式不同于蛋白质中侧链随机紧密堆积所预期的分布。它与氧-硫-芳香族相互作用相反，与芳香族-芳香族相互作用相似，几乎肯定起源于静电作用。
