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.
Keywords: molecular chaperones, heat shock proteins, hsp70, chaperonin
Protein & Peptide Letters
Title: Protein Folding Assisted by Chaperones
Volume: 12 Issue: 3
Author(s): Julio C. Borges and Carlos H.I. Ramos
Affiliation:
Keywords: molecular chaperones, heat shock proteins, hsp70, chaperonin
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.
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Cite this article as:
Borges C. Julio and Ramos H.I. Carlos, Protein Folding Assisted by Chaperones, Protein & Peptide Letters 2005; 12 (3) . https://dx.doi.org/10.2174/0929866053587165
DOI https://dx.doi.org/10.2174/0929866053587165 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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