Hemoglobin and Myoglobin

Question 1

Myoglobin

Answer 1

Binds oxygen in the muscle
monomer
only tertiary

Question 2

Hemoglobin

Answer 2

Binds oxygen in the lungs and stores in tissues
oligomer
has quaternary

Question 3

Oxygen binding to myoglobin

Answer 3

hyperbolic
constant affinity
high affinity
R state
independent of other molecules

Question 4

Oxygen binding to hemoglobin

Answer 4

sigmoidal
cooperative binding affinity
low to high affinity
T to R state

Question 5

Cooperative Binding Affinity

Answer 5

ligand affinity changes as more ligands bond - conformational change of shape

Question 6

T state

Answer 6

tense state
low affinity for o2
deoxy HB
larger central cavity

Question 7

R state

Answer 7

relaxed state
high affinity for o2
oxy HB
smaller central cavity

Question 8

Allostery

Answer 8

binding of a ligand at one site on a protein affects the binding of ligands at other sites
quaternary proteins more likely to experience

Question 9

Effectors

Answer 9

compounds which alter affinity at other binding sites upon binding

Question 10

Homoallosteric

Answer 10

affects binding of same compound

Question 11

Heteroallosteric

Answer 11

affects binding of different compound

Question 12

Activator

Answer 12

increases binding affinity e.g. O2

favours R state

Question 13

Inhibitor

Answer 13

decreases binding affinity e.g. BPG and H+

favours T state

Question 14

BPG

Answer 14

1 BPG binds to deoxyHB
stabilizes T state
negative heteroallosteric inhibitor of o2 binding