Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

4. Protein Structure

Chaperone Proteins

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Multiple Choice

Which of the following statements is false concerning Heat shock protein 60 (HSP60), a chaperonin protein.

HSP60 is required for some proteins to make their proper protein folding process spontaneous.

Like HSP70, HSP60 facilitates proper protein folding through binding & hydrolysis of ATP.

Cellular expression of HSP60 concentration increases in high temperature environments.

HSP60 operates by forming a large cage that the unfolded polypeptide enters to assume its native fold.

Previous problem

Verified step by step guidance

Understand the role of HSP60: Heat shock proteins like HSP60 are molecular chaperones that assist in the proper folding of proteins, especially under stress conditions such as high temperatures.

Analyze the statement about spontaneity: Protein folding is a complex process that often requires assistance from chaperones like HSP60. The statement that HSP60 makes the folding process spontaneous is misleading because chaperones facilitate folding but do not make it spontaneous.

Consider ATP involvement: HSP60, like HSP70, uses ATP binding and hydrolysis to facilitate the folding process. This energy input is crucial for the chaperone's function.

Evaluate the environmental response: The expression of HSP60 increases in response to stress conditions, such as elevated temperatures, to protect cells by ensuring proteins fold correctly.

Examine the structural mechanism: HSP60 operates by forming a large cage-like structure, providing an isolated environment for the unfolded polypeptide to fold into its native structure, which aligns with the known mechanism of action for chaperonins.