Some chaperone systems work as foldases: they support the folding of proteins in an ATP-dependent manner (for example, the GroEL/GroES or the DnaK/DnaJ/GrpE system). Although most newly synthesized proteins can fold in absence of chaperones, a minority strictly requires them for the same. Other chaperones work as holdases: they bind folding intermediates to prevent their aggregation, for example DnaJ or Hsp33. Chaperones can also work as disaggregases, which interact with aberrant protein assemblies and revert them to monomers. Some chaperones can assist in protein degradation, leading proteins to protease systems, such as the ubiquitin-proteasome system in eukaryotes. Chaperone proteins participate in the folding of over half of all mammalian proteins.
some chaperone systems work as foldases they support the folding of proteins in an atp-dependent manner (for example the groel/groes or the dnak/dnaj/grpe system) although most newly synthesized proteins can fold in absence of chaperones a minority strictly requires them for the same other chaperones work as holdases they bind folding intermediates to prevent their aggregation for example dnaj or hsp33 chaperones can also work as disaggregases which interact with aberrant protein assemblies and revert them to monomers some chaperones can assist in protein degradation leading proteins to protease systems such as the ubiquitin-proteasome system in eukaryotes chaperone proteins participate in the folding of over half of all mammalian proteins