MCQ on Molecular Chaperones

Molecular chaperones are proteins that assist in the proper folding, assembly, and stabilization of other proteins. They prevent misfolding and aggregation, guide proteins to their functional conformation, and can help refold or target damaged proteins for degradation. This is an MCQ on Protein Chaperones (MCQ on Molecular Chaperones).

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1. 
What are molecular chaperones primarily responsible for in cells?What are molecular chaperones primarily responsible for in cells?

2. 
Chaperone proteins help prevent protein misfolding and aggregation. What can occur when proteins misfold or aggregate?

3. 
Heat shock proteins (HSPs) are a well-known class of molecular chaperones. They are often upregulated in response to:

4. 
Chaperone proteins can interact with nascent (newly synthesized) polypeptides to assist in their proper folding. Which organelle is often involved in this process in eukaryotic cells?

5. 
Molecular chaperones are involved in maintaining protein homeostasis. What is the term commonly used to describe this cellular process?

6. 
Which class of molecular chaperones is responsible for facilitating the refolding of misfolded proteins or preventing their aggregation?

7. 
Which of the following is an example of a chaperone protein associated with the mitochondria and involved in the folding of proteins within this organelle?

8. 
Chaperone proteins can assist in protein transport and translocation across cellular membranes. This is particularly important in which of the following processes?

9. 
What is the main function of HSP90 chaperone proteins in cells?

10. 
Molecular chaperones can be involved in various cellular processes, including assisting in the folding of newly synthesized proteins and helping proteins recover from denaturation. What is denaturation?

11. 
Chaperone proteins often recognize and bind to exposed hydrophobic regions of unfolded or misfolded proteins. What is the term for these exposed hydrophobic regions?

12. 
Molecular chaperones are not only found in eukaryotic cells but also in prokaryotic cells (bacteria). What is the term often used to describe chaperone proteins in bacteria?

13. 
In addition to their role in protein folding, chaperone proteins are involved in the quality control of proteins. Which cellular structure is responsible for degrading misfolded or damaged proteins?

14. 
Chaperone proteins can also play a role in cellular responses to environmental stress. What is the term used to describe the overproduction of chaperones in response to stress?

15. 
The protein folding process can be complex, and chaperone proteins are essential for correct folding. What is the term for the final three-dimensional structure of a protein?

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MCQ on Molecular Chaperons




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