Below is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelledHb).Fraction of Hb bound with Oxygen1.00.80.60.40.20.002040pO2 (torr)6080ABCc. Which curve lacks cooperativity? [Select]Hb100a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no othersmall allosteric molecules associated)? [Select]b. Which curve has the lowest affinity (as measured by the p50)? [Select]

The pO2 in lungs is about 13.3 kPa, whereas in tissues it is 4kPa. A protein that carries oxygen to…

Answered: Below is the O₂ binding curve for adult…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The Bohr effect related to A. the ability of Hb to bind 02 in the presence of BPG. the ability of myoglobin to expel protons when binding 02. B. the ability of Hb to "take up" protons when binding 02. C. the ability of Hb to release protons when binding O2. D. O E. BPG ionization at 30 torr (the pO2 in veins).
O, saturation curve is shown beloww for hemoglobin at various pHs. Detail this Bohr effect from the molecular perspective. Be sure to include discussion of what causes this (i.e. specific amino acids), why the curves are right shifted with decreasing pH, and why this is logical in delivery of 02 to areas of higher demand. 100 Myoglobin 80- pH 7.6 60 pH 7.4 pll 7.2 40- pH 7.0 pH 6.8 20- Venous 0- 0. 20 10 60 80 Percent saturation
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Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain astructural variant of hemoglobin, HbF, consisting of two α and two γ subunits (α2 γ2 ), whereas maternal erythrocytes contain HbA (α2β2).(a) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain.(b) What is the physiological significance of the different O2 affinities?(c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2 -saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2 -saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of fetal and…
PTP1B Substrate kcat Km. kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEP YLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 + 0.22 0.53 + 0.02 34.7 + 0.25 52.7 + 0.7 0.066 + 0.001 ) The units for kcat/KM in the above are given according to standard scientific notation. On this (d) ( basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?
Given the following, calculate Gk: ENa = +45 mV; Ek = -85 mV; ECl = -60 mV; GNa = 5x10-8 S; GCl =0; Vm = -70 mV
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a. How many subunits does hemoglobin have? What are their conventional names? b. Identify the oxygen binding sites on hemoglobin. How many oxygens can one molecule of hemoglobin bind? How many oxygens can one subunit of hemoglobin bind? c. Identify the central cavity of hemoglobin. Is it the same or different than the oxygen binding site of hemoglobin?
Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector? a. Positive homotropic effector b. Negative homotropic effector c. Positive heterotropic effector d. Negative heterotropic effector
Give typed explanation Which of the following effects is NOT true? If stripped Hb is treated with 2,3-BPG, the O2-binding curve for Hb will shift left. If stripped Hb is treated with 2,3-BPG and CO2, the O2-binding curve for Hb will mirror that of fully intact Hb. If stripped Hb is treated with CO2, the O2-binding curve for Hb will shift right. All of the listed effects are true.
Why is the decreased affinity of fetal hemoglobin for BPG advantageous? With fewer BPG molecules bound to heme, there are more heme residues available for O2 binding. O A. B. Decreased BPG binding biases the fetal hemoglobin toward the R state. C. More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state. BPG is more available to bind to fetal myoglobin. helping to release O2 in fetal muscle tissue. D. 47
. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. F. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors O, release. H. Stabilization of the T-conformer favors O, release.

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