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Related Experiment Videos

Interior turns in globular proteins.

G D Rose, W B Young, L M Gierasch

    Nature
    |August 18, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Protein reverse turns, especially beta-turns, usually face outward. However, some buried turns were found to be stabilized by bound water molecules, integral to protein structure.

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    Area of Science:

    • Protein structure and dynamics
    • Biophysics
    • Structural biology

    Background:

    • Protein secondary structure includes reverse turns, which enable polypeptide chain direction changes.
    • Beta-turns are a specific type of reverse turn, characterized by four residues and a polar nature.
    • Typically, reverse turns are located on the protein surface, interacting with solvent water.

    Purpose of the Study:

    • To investigate the occurrence and structural role of buried reverse turns in proteins.
    • To understand the molecular mechanisms stabilizing these internal turns.

    Main Methods:

    • Analysis of protein structures with known three-dimensional coordinates.
    • Identification and characterization of reverse turns within protein interiors.
    • Examination of interactions between buried turns and surrounding solvent molecules.

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    Main Results:

    • Reverse turns are generally found at the protein surface.
    • In some cases, reverse turns were identified within the hydrophobic interior of proteins.
    • Buried turns were consistently found to be associated with bound solvent molecules.

    Conclusions:

    • Bound water molecules can play a crucial role in stabilizing otherwise atypical, buried reverse turns.
    • These water molecules are integral components of the protein's overall structure.
    • The findings expand the understanding of protein structural motifs and their stabilization mechanisms.