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Allosteric Effects

Allosteric Effects
The Hill coefficient (nH) for myoglobin and hemoglobin are respectively

1.0 and 2.8
1.2 and 4.5
4.5 and 1.2
2.8 and 1.0

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Allosteric Effects
A protein that binds two ligands in a non-cooperative manner will show

a linear Scatchard Plot
both (b) and (c)
a sigmodial binding curve
a hyperbolic binding curve

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Allosteric Effects
A protein that shows infinite cooperative for binding of n ligands will

both (b) and (c)
show a Hill coefficient (nH) of n
show a Hill coefficient (nH) of 0.0
only be found in either the unliganded form or the fully liganded form

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Allosteric Effects
An allosteric activator

decreases the binding affinity
increases the binding affinity
both (a) and (c)
stabilizes the R state of the protein

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Allosteric Effects
Small molecules affect hemoglobin (Hb) by

increasing Hb affinity for O2
increasing [H+] and decreasing Hb affinity for O2
decreasing Hb affinity for O2
increasing [H+]

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Allosteric Effects
In hemoglobin, allosteric effects occur

to minimize oxygen delivery to the tissues
only in humans
to maximize oxygen delivery to the tissues
for maintaining Fe in the Fe2+ state

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MORE MCQ ON Allosteric Effects

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