Detail Page

  • 1437867PublicAssets/3402When the heat shock protein hsp33 is folded, it is inactive and contains a zinc ion, stabilizing the redox sensitive domain (orange). In the presence of an environmental stressor, the protein releases the zinc ion, which leads to the unfolding of the redox domain. This unfolding causes the chaperone to activate by reaching out its "arm" (green) to protect other proteins.Dana Reichmann, University of MichiganUrsula Jakob and Dana Reichmann, University of MichiganVideo

    Topic Tags:

    Molecular Structures

    Hsp33 Heat Shock Protein Inactive to Active

    When the heat shock protein hsp33 is folded, it is inactive and contains a zinc ion, stabilizing the redox sensitive domain (orange). In the presence of an environmental stressor, the protein releases the zinc ion, which leads to the unfolding of the redox domain. This unfolding causes the chaperone to activate by reaching out its "arm" (green) to protect other proteins.

    Source

    Dana Reichmann, University of Michigan

    Credit Line

    Ursula Jakob and Dana Reichmann, University of Michigan

    Record Type

    Video

    ID

    3402

My Images/Videos