1) The plot to the right shows the Oxygen Saturation of Hemoglobin (Hb) versus O2 concentration. Draw a dashed curve on the figure to the right that represents how this mutation would likely change the curve. Note: that I am asking for how a change in affinity between HBa and HBB chains will impact HB binding to O2 a) The Kd between HBa and HBB chains is 100 nM. When L35S mutation (Leucine 35 → Serine) is introduced into the Hba chain Y 0.50 the Kd changes to 300 mm. 1.00 0.75 HB 0.25 HBg | 35S 0.00 0 2 4 pO₂ (kPa) b) How might this specific mutation alter the interaction between HBa and HBB chains? I am asking you to predict what Leu specifically might be doing here. 8 c) Now imagine that a second mutation is added to the HBa L35S mutant to generate an HBa L35S D101P double mutant. A measure of the double mutant shows that it has a Kd = 2 kPa, but does not change the binding of HBa and HBB. Draw a dotted line on the figure above that shows the resulting curve for the double mutant. d) For your graphs, estimate what percent of the O2 carried by HB would be delivered from your lungs (kPa= 13) to your tissues at rest (kPa = 4) and during exercise (kPa = 3) for each of the Hb variants. Comment on which one would be the most efficient at transporting O2. i) 10 Non&Can Cange Amor Boy

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Related questions

Question

1) The plot to the right shows the Oxygen
Saturation of Hemoglobin (Hb) versus O2
concentration.
a) The Kd between HBa and HBB chains is
100 nM. When L35S mutation (Leucine 35
→ Serine) is introduced into the Hba chain
the Kd changes to 300 mm.
\^^^^^A^A
Draw a dashed curve on the figure to the right
that represents how this mutation would likely
change the curve. Note: that I am asking for how
a change in affinity between HBa and HBB chains
will impact HB binding to O2
1.00
0.75-
HB
Y 0.50
HBa L35S
HBa L35S D101P
0.25
0.00
0
2
4
po₂ (kPa)
6
b) How might this specific mutation alter the interaction between HBa and HBB
chains? I am asking you to predict what Leu specifically might be doing here.
8
c) Now imagine that a second mutation is added to the HB¤ L35S mutant to
generate an HBa L35S D101P double mutant. A measure of the double mutant
shows that it has a Kg = 2 kPa, but does not change the binding of HBa and HBB.
Draw a dotted line on the figure above that shows the resulting curve for the
double mutant.
d) For your graphs, estimate what percent of the O2 carried by HB would be
delivered from your lungs (kPa= 13) to your tissues at rest (kPa = 4) and during
exercise (kPa = 3) for each of the Hb variants. Comment on which one would be
the most efficient at transporting O2.
i)
ii)
iii)
10

Expert Solution

Step 1

Oxygen saturation is a measure of how much hemoglobin is currently bound to oxygen compared to how much hemoglobin remains unbound. At the molecular level, hemoglobin consists of four globular protein subunits. Each subunit is associated with a heme group.

Two globin chains that have heme groups combine to form hemoglobin. One of the chains is an alpha chain and the other is a non-alpha chain. Non-alpha chain nature in hemoglobin molecules varies due to different variables. Fetuses have a non-alpha chain called gamma and after birth it is then called beta.

Oxyhaemoglobin is the haemoglobin bound to oxygen and oxygen is transported in this form to tissues from the lungs. The binding of oxygen to haemoglobin is reversible and oxygen dissociates in the tissues and gets released.

Each haemoglobin binds to four oxygen molecules. The binding of oxygen to haemoglobin is cooperative and reversible. The binding of oxygen primarily depends on pO2, pCO2, H+ concentration and temperature. The adult human haemoglobin.