Protein folding assisted by chaperones

Protein Pept Lett. 2005 Apr;12(3):257-61. doi: 10.2174/0929866053587165.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Chaperonins
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / metabolism*
  • Models, Molecular
  • Molecular Chaperones / metabolism*
  • Protein Folding*

Substances

  • Heat-Shock Proteins
  • Molecular Chaperones
  • Chaperonins