Chaperone proteins Slow atpases that bind newly synthesized proteins and assist their proper folding.
CHAPERONE PROTEINS - A series of proteins present in the endoplasmic reticulum which guide the proper folding of secreted proteins through a complex series of binding and release reactions.
In the absence of steroid hormone, the receptors cling together in a complex called aporeceptor complex, which also contains chaperone proteins (also known as heatshock proteins or Hsps).
Both Hsp27 and Hsp90-chaperone proteins have been implicated in increasing the activity of the ubiquitin-proteasome system, though they are not direct participants in the process.
 See also: Protein, Nucleus, Action, Membrane, Enzymes
  
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