ALLOSTERIC EFFECTS QUIZ

it is displaced from the heme by oxygen

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

its binding pocket becomes too small to accommodate BPG

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

decreasing Hb affinity for O2

increasing Hb affinity for O2

increasing [H+]

increasing [H+] and decreasing Hb affinity for O2

4.5 and 1.2

1.2 and 4.5

1.0 and 2.8

2.8 and 1.0

to minimize oxygen delivery to the tissues

only in humans

to maximize oxygen delivery to the tissues

for maintaining Fe in the Fe2+ state

a linear Scatchard Plot

a sigmodial binding curve

a hyperbolic binding curve

both (b) and (c)

only be found in either the unliganded form or the fully liganded form

both (b) and (c)

show a Hill coefficient (nH) of n

show a Hill coefficient (nH) of 0.0

None of these

2

not defined

1

extensive protein conformational change

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

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

both (a) and (b)

the presence of hydrating water molecules

the opposite chirality of the binding ligand

the amino acid residues lining the binding site

the absence of competing ligands

reorganization of protein-protein contacts between the individual subunits

binding of oxygen to the heme

movement of the proximal histidine towards the heme

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