Chapter 7 Hemoglobin

Question 1

allosteric protein

Answer 1

changes structure

Question 2

Affect ability of O2 to to bind to Hb

Answer 2

H, CO2, Cl-, BPG

Question 3

myoglobin structure

Answer 3

one peptide chain and one heme group. 8 regions of alpha-helix. polar side chains on surface. two histidine side chains in interior

Question 4

hemoglobin structure

Answer 4

a tetramer of two alpha chains and two beta chains

Question 5

myoglobin can bind ? O2

Answer 5

1

Question 6

first protein for which complete 3D structure was known

Answer 6

myoglobin

Question 7

When oxygen binds, Fe goes into ? plane

Answer 7

heme

Question 8

? helps minimize oxidation of Fe and prevents production of ROS/superoxide

Answer 8

distal histidine

Question 9

distal histidine decreases ? affinity, although it is still preferred to O2

Answer 9

CO

Question 10

Hb function

Answer 10

bind oxygen in lungs and release it in capillaries

Question 11

Hb demonstrates ? coopereativity

Answer 11

positive

Question 12

myoglobin/hemoglobin has higher O2 affinity

Answer 12

myoglobin

Question 13

hemoglobin has a ? binding curve

Answer 13

sigmoidal

Question 14

myoglobin has a ? binding curve

Answer 14

hyperbolic

Question 15

Bohr Effect

Answer 15

effect of pH on binding ability of Hb. Caused by competition between O2 and H+ binding.

Question 16

fetal Hb has lower affinity for ?

Answer 16

BPG