Question

How do Chaperones recognize proteins that are NOT completely folded?

1) Chaperones can recognize the shape of unfolded proteins.
2) Chaperones can recognize the shape of folded proteins.
3) Chaperones bind to patches of hydrophobic amino acids on other proteins.
4) Chaperones bind to patches of hydrophilic amino acids on other proteins.
5) Chaperones bind equally well to a folded or unfolded protein.

Answer 1

Option 3.

Chaperones identify incompletely folded proteins by binding to exposed hydrophobic amino acid patches, preventing aggregation and assisting in proper protein folding.

Step-by-step explanation:

Chaperones are specialized proteins that assist in the proper folding of other proteins within the cell.

They recognize proteins that are not completely folded by binding to patches of hydrophobic amino acids that are typically buried in the core of a properly folded protein but are exposed in unfolded or misfolded proteins.

Therefore, the correct option for how chaperones recognize proteins that are NOT completely folded is: 3) Chaperones bind to patches of hydrophobic amino acids on other proteins.

When a protein is newly synthesized or has been partially unfolded due to stress such as heat or changes in pH, these exposed hydrophobic regions can lead to aggregation with other proteins, which can be harmful to the cell.

Chaperones prevent this aggregation by shielding these regions, assisting the protein to achieve its correct conformation or refolding it back into the proper shape, ensuring that the proteins function properly.