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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

None of these
2
not defined
1

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Allosteric Effects
Small molecules affect hemoglobin (Hb) by

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

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

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

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Allosteric Effects
In hemoglobin, allosteric effects occur

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

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Allosteric Effects
An allosteric activator

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

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

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

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