Protein Folding Assisted by Chaperones
Julio C. Borges and Carlos H.I. Ramos
Affiliation: Centro de Biologia Molecular Estrutural, Laboratorio Nacional de Luz Sincrotron, CP 6192, 13084-971, Campinas, SP, Brazil.
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.
Keywords: molecular chaperones, heat shock proteins, hsp70, chaperonin
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