Chaperone proteins bind to mis-folded proteins to promote proper folding. To recognize misfolded proteins, the chaperone protein binds to: The signal sequence at the N-terminus of the misfolded proteinMannose-6-phosphate added in the GolgiPhosphorylated residues Hydrophobic stretches on the surface of the misfolded protein

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Chaperone proteins recognize misfolded proteins by binding to hydrophobic stretches on the surface of the misfolded protein.

Chaperone proteins are specialized proteins that assist in the proper folding of other proteins. They do this by recognizing and binding to misfolded proteins and helping them adopt their correct three-dimensional structure. The chaperone protein achieves this recognition by identifying hydrophobic stretches on the surface of the misfolded protein. These hydrophobic regions are typically buried within the core of the properly folded protein, so their exposure on the surface is an indication of misfolding. By binding to these hydrophobic stretches, chaperone proteins can prevent the misfolded protein from aggregating or becoming toxic, and facilitate its refolding into its native structure.

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