The allosteric effect of a regulator to an enzyme refers to A) binding of a regu

Question

The allosteric effect of a regulator to an enzyme refers to A) binding of a regulator affects the binding the substrate B) binding of substrate affect the binding of protein to a regulator C) binding of regulator affect the catalytic property of the enzyme D) covalent binding of regulator affect the binding of substrate E) binding of regulator affect covalent catalytic property of enzyme In hemoglobin, the transition from T state to R state (low to high affinity) is triggered by A) Fe^2+ binding to hemoglobin B) H^+ binding to hemoglobin C) O_2 binding to hemoglobin D) H_2 O binding to hemoglobin E) CO_2 binding to hemoglobin Carbon monoxide (CO) is toxic because: A) it binds to myoglobin and causes it to denature. B) it is rapidly converted to toxic CO_2. C) it binds to the globin's peptide portion and prevents the binding of O_2. D) it binds to the Fe^2+ in hemoglobin and prevents the binding of O_2. E) it binds to the N terminus of a peptide of hemoglobin and decrease its binding to O_2 Which of the following modulator's effect on binding of O_2 to hemoglobin is incorrect? A) H^+ acts as a negative heterotropic modulator B) CO_2 acts as a negative heterotropic modulator C) O_2 acts as a positive heterotropic modulator D) BPG acts as a negative heterotropic modulator E) CO acts as a competitive inhibitor Which of the following parts of the IgG (immunoglobulin G) molecule are not involved in binding to an antigen? A) Fab B) Fc C) Heavy chain D) Light chain E) variable domain

Explanation / Answer

1. A

Explanation: The allosteric interactions occur when binding of a ligand at particular site is effected by the binding of another ligand at site other than active one.

2. C

explanation: hemoglobin occurs in T state (tensed state) but when oxygen binds to hemoglobin it goes to R state.

3. D

explanation: because CO has a greater affinity for hemoglobin than oxygen.

4. E

Explanation: they are experimental facts

5.B

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