module 5

Question 1

Induced Fit

Answer 1

Changes in conformation that change the properties of a protein which changes its function

Question 2

Myoglobin

Answer 2

monomeric protein that stores oxygen in tissues

Question 3

Monomeric Protein

Answer 3

Proteins that combine to form multiple protein complexes

Question 4

Hemoglobin

Answer 4

Proteins that transport oxygen in red blood cells

Question 5

Oxygen solubility

Answer 5

Oxygen is hydrophobic

Question 6

Fe Six coordinating interactions

Answer 6

4 come with the heme rings
5 is an imidazole group of histidine one distal group (top) and one proximal group (bottom)
lastly an O that binds

Question 7

CO2 Poisoning

Answer 7

CO2’s got a lower affinity than Oxygen which means that Hem and Myo will actually bind to them instead of Oxygen

Question 8

Myoglobin

Answer 8

Tertiary structure with a heme group
Can bind to 1 oxygen

Question 9

Hemoglobin

Answer 9

Can bind to 4 oxygen
each subunit resembles a myoglobin

Question 10

Structure of myoglobin

Answer 10

single polypeptide with 153 residues arranged in 8 alpha helices
a heme group

Question 11

Oxygen Saturation curve for Myoglobin

Answer 11

3 torr is required to saturate 50% of myoglobin
we have 100 torr of oxygen in the lungs
20 torr in the lowest concentrations

Question 12

Saturated Oxygen Calculation

Answer 12

x= [pO2] / [pO2]/ [pO2] +[P50]
p50= 3 torr
Partial pressure of O2 in lungs is 100
In peripheral tissue is 20

Question 13

Hemoglobin Structure

Answer 13

Quaternary structure
contains red blood cells

Question 14

Allosteric Proteins

Answer 14

(Other structures)
T (inactive) and R (active) forms
T <—> R are in equilibrium

Question 15

Allosteric Modulators

Answer 15

Bind to allosteric proteins at specific sites
Allosteric activator stabilizes the R
Allosteric inhibitor stabilizes the T

Question 16

Homotropic

Answer 16

Modulator and Ligand are the same

Question 17

Heterotropic

Answer 17

Ligand and modulator are different

Question 18

T to R transition

Answer 18

T state in the iron atom is outside of the heme ring
R state moves iron into plane of heme ring

Question 19

2,3 Bisphospho-D-glycerate

Answer 19

An inhibitor for decreasing the affinity for oxygen in the hemoglobin

Question 20

O2 delivery and CO2 removal

Answer 20

CO2 is taken up by red blood cells and converted into bicarbonate and a proton is released
more protons = lower ph
lower pH will release more oxygen to the tissues

Question 21

O2 delivery and CO2 removal #2

Answer 21

CO2 Links to N terminus of each chain in Hemoglobin to form Carbaminohemoglobin
Carbamino Hemoglobin has lower O2 affinity than hemoglobin to promote O2 release

Question 22

Protons/ acids

Answer 22

More protons = decreased pH = lower oxygen affinity

Question 22

Sickle Cell Anemia

Answer 22

Change in single amino acid
Fibers form in capillaries which block blood flow

Question 23

Hemocyanin

Answer 23

Uses Copper rather than iron to transport oxygen
no heme ring in a group