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Related Experiment Videos

Flagellar hook protein from Salmonella SJ25.

H Kagawa, K Owaribe, S Asakura

    Journal of Bacteriology
    |January 1, 1976
    PubMed
    Summary

    Researchers purified Salmonella hook protein, finding its molecular weight is 43,000. Its amino acid composition closely matches E. coli hook protein, with low alpha-helix content.

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    Fish physiology and biochemistry·2013

    Area of Science:

    • Microbiology
    • Structural Biology
    • Protein Chemistry

    Background:

    • Bacterial flagella are complex motility structures.
    • Flagellar hooks are essential components connecting basal bodies to filaments.
    • Salmonella SJ25 flagellar hooks were used for protein purification.

    Purpose of the Study:

    • To obtain an immunochemically pure preparation of Salmonella hook protein.
    • To characterize the physical and chemical properties of the hook protein.

    Main Methods:

    • Acid disintegration of flagellar hooks.
    • Column chromatography for protein purification.
    • Sodium dodecyl sulfate-gel electrophoresis for molecular weight determination.
    • Amino acid composition analysis.
    • Circular dichroism spectroscopy.

    Main Results:

    • An immunochemically pure hook protein preparation was obtained.
    • The molecular weight of the hook protein was determined to be 43,000 Da.
    • The amino-terminal residue was identified as seryl.
    • Amino acid composition was similar to E. coli hook protein.
    • Circular dichroism spectra indicated very low alpha-helix content.

    Conclusions:

    • The purified Salmonella hook protein is structurally distinct from flagellin.
    • The protein's low alpha-helix content suggests a unique structural role in the flagellar hook.

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