ALLOSTERIC EFFECTS QUIZ

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

stabilizes the R state of the protein

both (a) and (c)

increases the binding affinity

decreases the binding affinity

1

2

None of these

not defined

for maintaining Fe in the Fe2+ state

only in humans

to maximize oxygen delivery to the tissues

to minimize oxygen delivery to the tissues

both (b) and (c)

a sigmodial binding curve

a linear Scatchard Plot

a hyperbolic binding curve

movement of the proximal histidine towards the heme

binding of oxygen to the heme

reorganization of protein-protein contacts between the individual subunits

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

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

show a Hill coefficient (nH) of n

both (b) and (c)

show a Hill coefficient (nH) of 0.0

4.5 and 1.2

1.0 and 2.8

2.8 and 1.0

1.2 and 4.5

extensive protein conformational change

both (a) and (b)

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