Regulation and Chaperonins - Biochemistry
Card 1 of 12
Proteins fold to their native state because .
Proteins fold to their native state because .
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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.
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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Which of the following statements about protein folding is incorrect?
Which of the following statements about protein folding is incorrect?
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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.
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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Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
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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.
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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Proteins fold to their native state because .
Proteins fold to their native state because .
Tap to reveal 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.
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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Which of the following statements about protein folding is incorrect?
Which of the following statements about protein folding is incorrect?
Tap to reveal 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.
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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Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
Tap to reveal 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.
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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Proteins fold to their native state because .
Proteins fold to their native state because .
Tap to reveal 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.
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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Which of the following statements about protein folding is incorrect?
Which of the following statements about protein folding is incorrect?
Tap to reveal 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.
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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Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
Tap to reveal 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.
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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Proteins fold to their native state because .
Proteins fold to their native state because .
Tap to reveal 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.
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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Which of the following statements about protein folding is incorrect?
Which of the following statements about protein folding is incorrect?
Tap to reveal 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.
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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Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
Proper folding of proteins often requires molecular chaperones. Which of the following is not true about molecular chaperones?
Tap to reveal 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.
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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