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Allosteric Effects

Allosteric Effects
When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is

not defined
2
1
None of these

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

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

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Allosteric Effects
The specificity of a ligand binding site on a protein is based on

the amino acid residues lining the binding site
the opposite chirality of the binding ligand
the absence of competing ligands
the presence of hydrating water molecules

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Allosteric Effects
In hemoglobin, allosteric effects occur

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

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

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

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Allosteric Effects
An allosteric activator

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

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MORE MCQ ON Allosteric Effects

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