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Processing of proteins is subject to quality control within the ER, which prevents improperly folded proteins...

Processing of proteins is subject to quality control within the ER, which prevents improperly folded proteins from reaching the cell surface. What are the typical fates of the misfolded proteins and which proteins play a role in this process?

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The misfolded or unfolded proteins will be disaggregated by disaggregating chaperones. These Chaperones favor the native protein folding by either as unfoldases, powerfully unfolding and untangling misfolded polypeptides from folded or aggregated proteins, or as holdase, requisition hydrophobic sites in misfolding polypeptides.

The HSP (heat shock proteins) 60,70, 90, and 100 are typically involved with the chaperones for the disaggregation of the unfolded proteins. Unfolding, stabilization of extended chains, disaggregation, folding, translocation across the membranes of the organelles, targeting substrates for degradation, regulation of the heat-shock reaction are the main functions of the HSP proteins.

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