Regulation and Chaperonins - Biochemistry

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Question

Proteins fold to their native state because __________.

Answer

Proteins do not have maximum entropy in their native state. Folding requires order which decreases entropy in the system. The energy toll needed for this decrease in entropy is more than made up with by the increase in bonds formed when the protein folds into its native state. Therefore, the native state of a protein has the lowest energy.

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Question

Which of the following statements about protein folding is incorrect?

Answer

Protein folding diseases usually occur when beta-sheets alpha-helices misfold and precipitate into alpha-helices beta-sheets. This can lead to aggregation of amyloid deposits in the brain and neuronal apoptosis. Creutzfeld-Jacob Disease (CJD) and bovine spongiform encephalopathy (BSE, or mad cow disease) are examples of protein folding diseases.

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Question

Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?

Answer

The correct answer is "their binding to unfolded proteins is a passive, energy-free process." All molecular chaperones work by repeatedly binding to and releasing hydrophobic segments of unfolded proteins. This process is not passive and requires energy from the hydrolysis of ATP, which is why all molecular chaperones are also ATPases. All chaperones are proteins and they range in size from monomers to large multisubunit proteins.

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