Packing constraints of hydrophobic side chains in (α/β)8 barrels

Authors

  • Nickolie Vtyurin,

    Corresponding author
    1. Department of Biopolymers Structure and Function Research, Institute of Molecular Genetics, Russian Academy of Sciences, 123182, Moscow, Russia
    • Department of Biopolymers Structure and Function Research, Institute of Molecular Genetics, Russian Academy of Sciences, Kurchatov sq., 123182, Moscow, Russia
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  • Victor Panov

    1. Department of Biopolymers Structure and Function Research, Institute of Molecular Genetics, Russian Academy of Sciences, 123182, Moscow, Russia
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Abstract

An analysis of possible tight packing of hydrophobic groups simultaneously at the both surfaces of β-hyperboloid-8 was conducted. This analysis shows that the disposition of amino acid side chains at the real β-structure's surface is unique. If we sign the mean distance between adjacent β-strands as “a,” and the mean distance along β-strand between Cα atoms, whose side chains are directed to one side of the β-sheet, as “b,” the ratio b/a = √2 very precisely. This ratio ensures the most efficient packing of side hydrophobic groups at the outer surface of β-hyperboloid-8, forming, at the same time, the second by efficiency packing at its inner surface. © 1995 Wiley-Liss, Inc.

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