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How does a chaperone work with proteins?

a) By breaking peptide bonds
b) By assisting in protein folding
c) By promoting transcription
d) By inhibiting translation

1 Answer

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Final answer:

Chaperones assist proteins by aiding in their correct folding to ensure their functional three-dimensional structure. The correct answer is option b).

Step-by-step explanation:

Chaperones work with proteins by assisting in protein folding. They are helper molecules that associate with the target protein during its folding process to prevent the aggregation of polypeptides. This is crucial since aggregation can lead to misunderstandings in the protein's structure and potentially a dysfunctional shape.

Once the target protein is properly folded, chaperones disassociate from it, having performed their role in aiding in the correct three-dimensional structure of the protein. Conditions such as abnormal temperature or pH can hinder a protein's ability to fold spontaneously, but chaperones help to mitigate these effects, thereby ensuring functional proteins.

Such conditions can be detrimental to proteins, but chaperones help to protect the protein's structure during these times. By preventing aggregation and promoting proper folding, chaperones help proteins avoid misfolding and potential dysfunction. They play an important role in maintaining protein homeostasis within cells.

User Akshay Garg
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