MCQ on Heat Shock Proteins (HSPs)

Heat shock proteins (HSPs) are a family of cellular proteins that help cells respond to stress, such as high temperatures or other environmental challenges. They assist in protein folding, prevent damage, and facilitate the removal of damaged proteins, promoting cell survival under adverse conditions. This is an MCQ on Heat Shock Proteins (HSPs)

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1. 
Heat shock proteins (HSPs) are named after their initial discovery in response to what type of stress?

2. 
What is the primary function of heat shock proteins in cells?

3. 
Which class of heat shock proteins is often involved in preventing protein aggregation and refolding denatured proteins?

4. 
In which cellular compartment are HSPs often involved in assisting in protein folding and preventing aggregation?

5. 
What is the main function of HSP90 chaperone proteins in cells?

6. 
HSP60 chaperone proteins are often associated with which cellular organelle and are involved in the folding of proteins within this organelle?

7. 
Molecular chaperones, such as heat shock proteins, can interact with nascent (newly synthesized) polypeptides to assist in their proper folding. What is the term for these nascent polypeptides before they are fully functional proteins?

8. 
Heat shock proteins, such as HSP70, can recognize and bind to exposed hydrophobic regions of unfolded or misfolded proteins. What is the term for these exposed hydrophobic regions?

9. 
Which class of HSPs is responsible for facilitating the refolding of misfolded proteins or preventing their aggregation?

10. 
Heat shock proteins are involved in the cellular response to a variety of stresses, including environmental factors and disease. What term describes the overproduction of HSPs in response to stress?

11. 
Heat shock proteins are not only found in eukaryotic cells but also in prokaryotic cells (bacteria). What is the term used to describe chaperone proteins in bacteria?

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MCQ on Heat Shock Proteins (HSPs)




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