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The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation). The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure. The chemical reactions and pathways involving macromolecules, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, as carried out by individual cells. The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. Oxidation of two organic sulfhydryl groups (thiols) by a disulfide compound to form a disulfide bond. Completion of folding of alpha- and beta-tubulin; takes place subsequent to chaperonin-mediated partial folding; mediated by a complex of folding cofactors. The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes protein modification. The chemical reactions and pathways involving a specific protein, rather than of proteins in general. Includes protein modification. The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that results in the attainment of the full functional capacity of a protein.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein folding
Acc: GO:0006457
Aspect: Biological Process
Desc: The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
Synonyms:
  • chaperonin-mediated tubulin folding
  • chaperone activity
  • co-chaperone activity
  • GO:0007022
  • co-chaperonin activity
  • GO:0007025
  • GO:0007024
  • protein complex assembly, multichaperone pathway
  • chaperonin ATPase activity
  • glycoprotein-specific chaperone activity
  • non-chaperonin molecular chaperone ATPase activity
  • alpha-tubulin folding
  • beta-tubulin folding
Proteins in PDR annotated with:
   This term: 1228 [Search]
   Term or descendants: 1349 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0006457 - protein folding (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle