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CH436A Problem Set #2
Fetal hemoglobin (HbF), which contains 20 Î±2Î³ subunits, is made in the body until about an age of this time; HbF subunits are replaced by adult hemoglobin (HbA), which contains Î±2Î²2. HbF has a higher binding affinity for O2 than HbA, and because of this, the fetus is able to take oxygen from the mother’s blood.
The following plot shows binding = HbA + HbF, with and without 2,3-BPG present. For HbA, label the conditions on the graph most closely associated with the R state and the T state. Put next to the condition with the highest P50 value.
pO2 (Pa)
It turns out that HbF has an AA substitution of Histidine (in HbA) to Serine (in HbF) – Yes, the same Histidine in the 2,3-BPG binding pocket of the Hb in problem #2.
1) Why does this substitution change 2,3-BPG binding to HbF vs HbA?
2) How does this explain the graph above?

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01:16

Fetal hemoglobin (HbF) contains serine instead of histidine atposition 143 of the g chain which is the equivalent of the adulthemoglobin (HbA) b chain. Position 143 faces the central cavitybetween the g chains.1. Why does 2,3-bisphosphoglycerate (BPG) bind more tightlyto deoxy HbA than to deoxy HbF?2. How does the decreased affinity of HbF for BPG affectthe affinity of HbF for O2?3. The P50 for HbF is 18 torr and the P50 for HbA is 26torr. How do these values explain the efficient transfer of oxygenfrom maternal blood to the fetus?

05:37

The graph below represents the adult hemoglobin binding curve at pH 7 in the presence of 2,3-bisphosphoglycerate: The hemoglobin binding curve has a sigmoidal shape, due to four interacting oxygen-bound sites. For comparison, the myoglobin binding curve only has one oxygen-bound site and has a hyperbolic curve. Given the five scenarios shown, determine which shift would occur in the hemoglobin binding curve. Circle RS (right shift) or LS (left shift) (10 points)

L- AyejlL ob` exejl HaHemoglobin is isolated from red blood cells and stripped of BPGRS LSThe blood pH drops from pH 7.4 to 7.2RS LSThe carbon dioxide concentration of the blood increasesRS LSThe adult hemoglobin is replaced by fetal hemoglobinRS LSTetrameric hemoglobin is dissociated into its subunitsRS LSP 02

05:20

Consider the following hemoglobin saturation profile with three curves: A, Normal Hb, and 1.0. The middle curve is representative of normal HbA at normal atmospheric conditions.

Which curve shows the lowest affinity for oxygen?

b) Which curve would represent O2 binding to hemoglobin if the pH dropped from 7.4 to 7.22?

c) If a mutation was made that stabilized the R-state, which curve would most likely be representative of oxygen binding for the mutant?

d) If a mutation was made in the central cavity of Hb that caused decreased binding of 2,3-BPG, would oxygen affinity increase or decrease?

e) If you are going to live in a very low oxygen environment, which curve would you want your Hb to follow? Curve A, Normal Hb, or Curve C? Why?

f) The distal site histidine that interacts with the heme in hemoglobin is mutated to an alanine. Predict which curve would most closely match the O2 affinity curve for this mutant.

02:49

The hemoglobin (Hb) variant Asp99Asn mutant, in which the aspartate position 99 of the beta subunit is replaced with asparagine. The binding curve for this variant is shown below versus the binding curve for the native Hb (the inset figure examines the region between pO2 of 0 and 40 torr based on the figure below). What is the effect of the mutation on the binding properties of Hb?

Based on the figure, where aspartate 99 (A99) more highly hinders what is function?

Ihia Kdoi N9gn9aMaClam MWaaltThe shape demonstrates the Bohr effect on hemoglobin.The Hill coefficient (n) for Asp99Asn Hb is lower than that for native Hb.

Asparagine binds less O2 at certain partial pressures than native Hb.Aspartate

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