Skip to main content

Protein Folding Assisted by Chaperones

Buy Article:

$55.00 plus tax (Refund Policy)

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.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: chaperonin; heat shock proteins; hsp70; molecular chaperones

Document Type: Review Article

Affiliations: Centro de Biologia Molecular Estrutural, Laboratorio Nacional de Luz Sincrotron, CP 6192, 13084-971, Campinas, SP, Brazil.

Publication date: 2005-04-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more