Amino-aromatic interactions in proteins.

S K Burley; G A Petsko

doi:10.1016/0014-5793(86)80730-x

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PubMed · 3089835

Amino-aromatic interactions in proteins.

S K Burley·G A Petsko

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Abstract

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.

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Arginine Asparagine Crystallography Glutamine Histidine Lysine Proteins Journal Article Research Support, Non-U.S. Gov't

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S K Burley, G A Petsko. 1986-07-28. Amino-aromatic interactions in proteins.. https://doi.org/10.1016/0014-5793(86)80730-x

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