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Questions and Answers
Which type of protein function involves altering the chemical configuration or composition of a bound molecule?
Which of the following is true about ligands?
Protein-ligand interactions are specific because...
What is the role of conformational changes in proteins?
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How do proteins interact with ligands?
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What is the significance of protein-ligand interactions in maintaining order in a living system?
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What is the range of conformational changes in proteins?
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Which of the following best describes the principle of induced fit?
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Which of the following is true about multisubunit proteins?
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What is the term used to describe the reversible binding of other molecules by a protein?
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What are the coordination bonds of iron in a heme prosthetic group?
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What is the role of myoglobin in the body?
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How can protein-ligand interactions be described quantitatively?
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What does the association constant (Ka) measure?
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Which state of hemoglobin has a higher affinity for oxygen?
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What triggers a conformational change from the T state to the R state in hemoglobin?
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What type of binding curve does hemoglobin exhibit for oxygen?
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What is the purpose of hemoglobin binding oxygen cooperatively?
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What is the Hill coefficient in the Hill equation used for?
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What does a Hill coefficient greater than 1 indicate in a Hill plot?
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What type of modulator is carbon monoxide for hemoglobin?
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What is the purpose of ion pairs in stabilizing the T state of hemoglobin?
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What is the effect of oxygen binding on the conformation of hemoglobin?
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Which of the following correctly defines the dissociation constant (Kd)?
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Which of the following statements about the binding affinity of a ligand is true?
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What is the value of Kd when 50% of the ligand-binding sites are occupied?
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Which of the following correctly describes the effect of protein structure on ligand binding?
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What is the primary reason for carbon monoxide (CO) binding more strongly to free heme than oxygen (O2)?
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What is the role of the distal histidine (His) in myoglobin?
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Which of the following best describes the quaternary structure of hemoglobin?
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Which of the following statements is true about the dissociation constant (Kd)?
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What is the relationship between Kd and affinity?
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What is the role of Myoglobin's distal His in increasing heme's affinity for O2?
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What is the main function of erythrocytes (red blood cells)?
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How many subunits does adult hemoglobin have?
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What type of interaction is responsible for the quaternary structure of hemoglobin?
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What is the term for the structural adaptation that occurs between a protein and a ligand?
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