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Amino-aromatic interactions in proteins.

S K Burley, G A Petsko

    FEBS Letters
    |July 28, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Amino groups in proteins preferentially interact with aromatic side chains, specifically targeting pi-electrons. This electrostatic interaction pattern, observed in high-resolution structures, differs from random packing and other aromatic interactions.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Computational Biology

    Background:

    • Protein structure is determined by the spatial arrangement of amino acid side chains.
    • Interactions between amino acid side chains are crucial for protein folding, stability, and function.
    • Aromatic side chains (phenylalanine, tyrosine, tryptophan) and amino groups (lysine, arginine, asparagine, glutamine, histidine) are common in proteins.

    Purpose of the Study:

    • To investigate the geometric preferences of amino group-aromatic side chain interactions in high-resolution protein crystal structures.
    • To determine if these interactions deviate from random spatial distributions.
    • To compare amino group-aromatic interactions with other known side chain interactions.

    Main Methods:

    • Geometric analysis of 33 high-resolution (≥2 Å) protein crystal structures.

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  • Analysis of the spatial proximity between positively charged amino groups and aromatic ring centroids.
  • Comparison of observed distributions with random close packing models.

    • Main Results:

    • Positively charged amino groups are preferentially located within 6 Å of aromatic ring centroids.
    • Amino groups interact with the pi-electron clouds (delta-) of aromatic rings, avoiding the ring edges (delta+).
    • This interaction pattern is distinct from random packing and contrasts with oxygen/sulfur-aromatic interactions, but resembles aromatic-aromatic interactions.

    Conclusions:

    • A specific, non-random geometric preference exists for amino group-aromatic side chain interactions in proteins.
    • These interactions are likely electrostatic in nature, driven by favorable contacts with pi-electron systems.
    • The findings contribute to understanding the forces governing protein structure and molecular recognition.