Chaperone
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Chaperones
Although the three-dimensional (tertiary) structure of a protein is determined by its primary structure, it may need assistance in achieving its final shape.
Chaperone
A protein that facilitates the folding of other proteins or assembly of multi-protein complexes.
Chaperone: Any cellular protein that binds to an unfolded or partially folded target protein to prevent misfolding, aggregation, and/or degradation of it.
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.
Chaperone (← links)
Chaperonin (← links)
Signatures (← links)
Signature sequence (← links)
Leader sequence (← links)
Secretory proteins (← links)
Streptovaricins (← links)
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Elongation factor (← links) ...
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), ...
In addition to protein synthesis, the rough endoplasmic reticulum also functions in the modification of newly formed proteins. For example, some enzymes may add carbohydrate chains forming glycoproteins. Molecular chaperones are enzymes that ...
 See also: Protein, Proteins, Trans, Cell, Cells
  
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