A) Each subunit can exist in a relaxed (R) and taut (T) conformation.
B) All subunits will be in either the R or the T conformation at the same time.
C) Some subunits can be in the R state while others are in the T state.
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A) The apparent KM for the substrate increases.
B) The apparent KM for the substrate decreases.
C) The apparent Vmax for the substrate increases.
D) The apparent Vmax for the substrate decreases.
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A) They are usually fully active in the form we eat them
B) They are usually water soluble
C) Niacin and riboflavin are examples
D) They are important in many metabolic reactions
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A) all subunits are in the R state.
B) all subunits are in the T state.
C) there is a 50:50 mix of R & T states.
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A) ATP inhibits and CTP activates
B) ATP activates and CTP inhibits
C) Both ATP and CTP inhibit
D) Both ATP and CTP activate
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A) Those with hydrophilic, neutral side-chains.
B) Those with negatively charged side-chains.
C) Those with positively charge side-chains.
D) Those with hydrocarbon side-chains.
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A) Feedback inhibition by product.
B) Addition or removal of phosphate groups from of the enzyme.
C) Presence of activators.
D) Activation of zymogens.
E) All of these regulate enzyme activity.
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A) substrate, activators, and inhibitors all compete for the same binding site on the enzyme.
B) there is no distinction between catalytic and regulatory subunits.
C) the presence of an activator makes the plot of reaction rate against substrate concentration less cooperative.
D) the presence of an inhibitor makes the plot of reaction rate against substrate concentration less cooperative.
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A) are not involved in reactions of carbohydrates.
B) play an insignificant role in generating energy.
C) are important processes in prokaryotes, but not in eukaryotes.
D) can be combined to afford a high degree of control over enzymatic reactions.
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A) Myoglobin
B) Hemoglobin
C) Chymotrypsin
D) Both hemoglobin and chymotrypsin.
E) All of these.
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A) the conformational change in the enzyme in one model and not in the other.
B) the number of predicted binding sites on the enzyme.
C) the manner in which changes in quaternary structure take place.
D) the response of the enzyme to changes in temperature.
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A) an enzyme inhibitor used in smoking cessation programs.
B) an inhibitor of ATP production.
C) a coenzyme in reactions that transfer acyl groups.
D) a coenzyme in oxidation-reduction reactions.
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A) they block the active site of enzymes so that inhibitors cannot bind.
B) they can act as Lewis acids.
C) water is excluded from the active site when metal ions are bound.
D) they prevent protein aggregation.
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A) obtaining a crystalline sample of the enzyme.
B) insuring that metal ions are always excluded from the enzyme sample.
C) determining the active site residues.
D) none of these
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A) it is always possible to define a KM
B) it is always possible to define a Vmax
C) competitive inhibition is always a possibility
D) much of the terminology is completely unchanged
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A) similar overall structures.
B) serine in their active sites.
C) histidine in their active sites.
D) active sites that can catalyze the reactions in question.
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