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Amino‐aromatic interactions in proteins

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Burley, S.K., Petsko, G.A.·1986·FEBS Letters

Abstract

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.

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Metadata

Authors
Burley, S. K., & Petsko, G. A.
Venue
FEBS Letters
Publisher
Wiley
Published
1986-07-28
Volume
203
Issue
2
Pages
139-143
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2080796053
Cited by
759
References
0
FWCI
8.99
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Amino‐aromatic interactions in proteins. https://app.cochat.ai/papers/10.1016/0014-5793(86)80730-x
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Burley, S. K., & Petsko, G. A. (1986). Amino‐aromatic interactions in proteins. FEBS Letters. https://doi.org/10.1016/0014-5793(86)80730-x

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