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Amino‐aromatic interactions in proteins
Author(s) -
Burley S.K.,
Petsko G.A.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80730-x
Subject(s) - side chain , chemistry , aromatic amino acids , phenylalanine , amino acid , histidine , van der waals force , tryptophan , ring (chemistry) , crystallography , asparagine , stereochemistry , organic chemistry , biochemistry , molecule , polymer
Geometric analysis of 33 refined high‐resolution protein crystal structures (2 Å or higher) demonstrates that side‐chain amino groups interact with aromatic side chains. Positively charged or δ(+) amino groups of lysine, arginine, asparagine, glutamine and histidine are preferentially located within 6 Å of the ring centroids of phenylalanine, tyrosine and trytophan, where they make van der Waals' contact with the δ(−) π‐electrons and avoid the δ(+) 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.