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Beta-pleated sheets in oligopeptide crystals

T Ashida, I Tanaka, T Yamane

    International Journal of Peptide and Protein Research
    |March 1, 1981
    PubMed
    Summary
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    Oligopeptide crystals commonly form beta-pleated sheet structures, exhibiting variations in chain arrangements and twists. Structural analysis reveals deviations from established models, particularly in heavily twisted sheets.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Crystallography

    Background:

    • Oligopeptide crystals frequently adopt beta-pleated sheet conformations.
    • Both parallel and antiparallel, as well as flat and twisted, sheet types are observed.

    Purpose of the Study:

    • To analyze structural parameters of oligopeptide beta-pleated sheets.
    • To compare observed parameters with established models like Pauling & Corey's.

    Main Methods:

    • Crystallographic analysis of oligopeptide structures.
    • Measurement and comparison of key structural parameters (angles, torsion angles, bond lengths, spacings).

    Main Results:

    • Observed structural parameters deviate significantly from Pauling & Corey predictions.

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  • Heavily twisted sheets exhibit greater twists than globular proteins, with near-perpendicular chains.
  • Torsion angles in twisted sheets resemble poly (L-proline) II helix.

    • Conclusions:

    • Oligopeptide beta-pleated sheet structures display significant structural diversity.
    • Existing models may not fully capture the conformational variability in these systems.
    • Deviations in T (NA alpha C') angles are influenced by main and side chain structures.