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  2. Dictionary

    chap·er·o·nin
    [ˌSHapəˈrōnən]
    noun
    biochemistry
    chaperonin (noun) · chaperonins (plural noun)
    1. a protein that aids the assembly and folding of other protein molecules in living cells.
    Origin
    1990s: from chaperone + -in.
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    Chaperonin | Wikipedia

    HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein … See more

    The structure of these chaperonins resemble two donuts stacked on top of one another to create a barrel. Each ring is composed of either … See more

    Chaperonins undergo large conformational changes during a folding reaction as a function of the enzymatic hydrolysis of ATP as well as binding of substrate proteins and … See more

    As mentioned, all cells contain chaperonins.
    • In bacteria, the archetype is the well-characterized chaperonin GroEL from E. coli.
    • In archaea, the chaperonin is called the thermosome See more

    Group I
    Group I chaperonins (Cpn60) are found in bacteria as well as organelles of endosymbiotic origin: chloroplasts and mitochondria.
    The GroEL/GroES complex in E. coli is a Group I chaperonin … See more

    Human GroEL is the immunodominant antigen of patients with Legionnaire's disease, and is thought to play a role in the protection of the … See more

    Human genes encoding proteins containing this domain include:
    BBS10
    • CCT1; CCT2; CCT3; CCT4; CCT5; CCT6A; CCT6B; CCT7; CCT8
    • CESK1
    See more

     
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