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Related Experiment Videos

The reverse turn as a polypeptide conformation in globular proteins.

J L Crawford, W N Lipscomb, C G Schellman

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1973
    PubMed
    Summary

    Globular proteins feature reverse turns, a common tertiary structure. These turns comprise 33% of amino acids, with specific amino acid preferences observed in their sequences.

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    Area of Science:

    • Protein structure and conformation
    • Biophysics
    • Structural biology

    Background:

    • Tertiary protein structure is crucial for function.
    • Reverse turns are a significant, yet under-characterized, protein motif.
    • Understanding turn formation aids in predicting protein folding and function.

    Purpose of the Study:

    • To define and quantify reverse turns in globular proteins.
    • To analyze the amino acid composition of reverse turns.
    • To compare the prevalence of turns with helices and beta-sheets.

    Main Methods:

    • Definition of reverse turns using dihedral angles and distance metrics.
    • Analysis of 125 reverse turns across seven globular proteins.
    • Statistical survey of amino acid distribution within turns.

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    Main Results:

    • Reverse turns constitute 33% of amino acids in analyzed proteins.
    • Amino acid composition: Asn and Gly are prevalent in turns, Pro in turns and helix initiation, Glu in helices.
    • Specific positional preferences: Asp (1st), Pro (2nd), Asn (3rd), Trp (4th) in turns.

    Conclusions:

    • Reverse turns are a major structural element in globular proteins.
    • Distinct amino acid preferences and positional biases exist within reverse turns.
    • This detailed analysis provides insights into protein folding and tertiary structure.