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.
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For the person who accompanies another during social situations, see chaperon.
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).
An example of an important endoplasmic reticulum resident protein is the chaperone protein known as BiP (formally: the chaperone immunoglobulin-binding protein), ...
 See also: Trans, Translation, Chaperone, Membrane, Nucleus
  
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