Defective proteins fail to function normally, most often because they fold improperly, forming an unstable or improper structure. Misfolded proteins are identified and bound by molecules called chaperones. If a protein cannot be folded properly, what happens to it?

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If correct folding does not occur, the chaperones remain irreversibly bound to the misfolded proteins, resulting in the sequestration of such proteins in the ER.

If correct folding does not occur, the chaperones remain bound to the misfolded proteins and direct the defective proteins to the peroxisomes.

If correct folding does not occur, the chaperones dissociate from the misfolded proteins and are sent to the lysosome for degradation.

If correct folding does not occur, the chaperones remain bound to the misfolded proteins and direct the defective proteins into vesicles for export outside of the cell.

 

asked May 15, 2013 in Genetics by GeneX ~Top Expert~ (7,947 points)
    

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If correct folding does not occur, the chaperones remain irreversibly bound to the misfolded proteins, resulting in the sequestration of such proteins in the ER.
answered May 15, 2013 by GeneX ~Top Expert~ (7,947 points)

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