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Related Experiment Videos

Multidomain of flagellin.

O V Fedorov, N N Khechinashvili, R Kamiya

    Journal of Molecular Biology
    |May 5, 1984
    PubMed
    Summary

    Salmonella flagellin monomers possess a multidomain structure. Polymerization into flagella involves domain rearrangement, with distinct structural changes observed during heating and cooling cycles.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Microbiology

    Background:

    • Flagellins are the primary protein subunits of bacterial flagella.
    • Understanding flagellin structure is crucial for bacterial motility and pathogenesis.

    Purpose of the Study:

    • To investigate the structural properties of normal and mutant Salmonella flagellins.
    • To elucidate the relationship between flagellin polymerization and thermal denaturation.

    Main Methods:

    • Scanning microcalorimetry to measure thermal transitions.
    • Circular dichroism spectroscopy to assess protein secondary structure.

    Main Results:

    • Flagellin monomers exhibit reversible thermal denaturation.
    • Calorimetric and van't Hoff enthalpies suggest two independent co-operative melting regions in monomers.
    • Circular dichroism indicates distinct structural differences between flagellin polymers and monomers.

    Conclusions:

    • Flagellin molecules possess a multidomain structure.
    • Polymerization into flagella induces structural changes in specific domains.
    • Two domains are structured in monomers, while others gain regularity upon polymerization.

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