ALLOSTERIC EFFECTS QUIZ

the opposite chirality of the binding ligand

the absence of competing ligands

the amino acid residues lining the binding site

the presence of hydrating water molecules

not defined

None of these

1

2

it is displaced from the heme by oxygen

BPG binds to the R state with the same affinity as the T state

it is displaced from the heme by movement of the proximal histidine

its binding pocket becomes too small to accommodate BPG

only in humans

to maximize oxygen delivery to the tissues

for maintaining Fe in the Fe2+ state

to minimize oxygen delivery to the tissues

increases the binding affinity

both (a) and (c)

decreases the binding affinity

stabilizes the R state of the protein

reorganization of protein-protein contacts between the individual subunits

movement of the proximal histidine towards the heme

binding of oxygen to the heme

movement of the F-helix, which contains the proximal His

both (a) and (b)

extensive protein conformational change

100-fold higher affinity for the last O2 bound than for the first

100-fold lower affinity for the last O2 bound than for the first

1.0 and 2.8

4.5 and 1.2

1.2 and 4.5

2.8 and 1.0

both (b) and (c)

a sigmodial binding curve

a hyperbolic binding curve

a linear Scatchard Plot

increasing Hb affinity for O2

increasing [H+] and decreasing Hb affinity for O2

increasing [H+]

decreasing Hb affinity for O2