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Multiple Choice
Heat shock protein 70 (HSP70), a chaperone protein found in many organisms, is one of the most highly conserved proteins in all of biology. Which of the following statements about HSP70 is true?
A
HSP70 operates by forming a large cage around the unfolded polypeptide to increase its solubility.
B
HSP70 facilitates proper protein folding without the use of energy.
C
Cellular expression of HSP70 concentration significantly increases in high temperature environments.
D
Expression of HSP70 concentration decreases or stays constant in high temperature environments.
Verified step by step guidance
1
Understand the role of HSP70: Heat shock proteins like HSP70 are molecular chaperones that assist in the proper folding of proteins, especially under stress conditions such as elevated temperatures.
Analyze the statement about HSP70 forming a large cage: This description is more characteristic of chaperonins like GroEL/GroES, not HSP70. HSP70 works by binding to nascent or unfolded polypeptides to prevent aggregation.
Consider the energy requirement: HSP70 requires ATP to function. It binds and releases polypeptides in an ATP-dependent manner, facilitating proper folding.
Evaluate the statement about expression levels: HSP70 expression is upregulated in response to stress conditions, such as high temperatures, to protect cells by ensuring proteins fold correctly.
Conclude with the correct statement: The statement 'Cellular expression of HSP70 concentration significantly increases in high temperature environments' is true, as it aligns with the known function of HSP70 in stress response.