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Amino Acids, Peptides, and Proteins > Proteins > Molecular Chaperones > Heat-Shock Proteins > Chaperonins
... > Enzymes and Coenzymes > Enzymes > Hydrolases > Acid Anhydride Hydrolases > Adenosine Triphosphatases > Chaperonins

Preferred term

Chaperonins  

Type

  • Topical Descriptor

Broader concept

Narrower concepts

Entry terms

  • Chaperonin
  • Chaperonin Family

Note

  • general or unspecified; prefer specifics

Scope note

  • A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.

History note

  • 95; was CHAPERONIN FAMILY (NM) 1989-94

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URI

http://www.yso.fi/onto/mesh/D018833

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RDF/XML TURTLE JSON-LD Created 5/31/94, last modified 5/27/20