title: Protein folding assisted by chaperones.
abstract: Molecular chaperones are one of the most important cell defense mechanisms against protein aggregation and misfolding. These specialized proteins bind non-native states of other proteins and assist them in reaching a correctly folded and functional conformation. Chaperones also participate in protein translocation by membranes, in the stabilization of unstable protein conformers and regulatory factors, in the delivery of substrates for proteolysis and in the recovery of proteins from aggregates.
authors.affiliation: Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Síncrotron, CP 6192, 13084-971, Campinas, SP, Brazil.
authors.forename: Júlio C
authors.initials: JC
authors.lastname: Borges
authors.forename: Carlos H I
authors.initials: CH
authors.lastname: Ramos
mesh_terms: D018833:Chaperonins; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D018833:Chaperonins