The chaperone Hsp60 recognizes potentially misfolded proteins by attracting expo

Question

The chaperone Hsp60 recognizes potentially misfolded proteins by attracting exposed hydrophobic regions of proteins. Why do you think this is the case?

Hsp60 is a barrel shaped protein that acts as a chaperone, and generates ATP if hydrophobic regions of proteins are bound.

Hydrophobic regions should be buried within proteins in the cytosol--if they are exposed it indicates that the protein is likely misfolded.

Since hydrophobic regions are normally found on the outside of proteins in the cytosol, these are the regions that would be easiest to bind.

Hsp60 s cap (GroES) binds hydrophobic regions of proteins.

All of the above statements are true.

Hsp60 is a barrel shaped protein that acts as a chaperone, and generates ATP if hydrophobic regions of proteins are bound.

Hydrophobic regions should be buried within proteins in the cytosol--if they are exposed it indicates that the protein is likely misfolded.

Since hydrophobic regions are normally found on the outside of proteins in the cytosol, these are the regions that would be easiest to bind.

Hsp60 s cap (GroES) binds hydrophobic regions of proteins.

All of the above statements are true.

Explanation / Answer

All of the above statements are true.

HSP60 are molecular chaperone and plays important role in regulating the folding, translocation, and assembly of native proteins. They identify proteins with abnormally exposed hydrophobic residues and form stable inactive aggregates after association. Exposed hydrophobic regions help in HSP70 recognition and subsequent reorganization.

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