O, saturation curve is shown beloww for hemoglobin at various pHs. Detail this Bohreffect 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 logicalin delivery of 02 to areas of higher demand.100Myoglobin80-pH 7.660pH 7.4pll 7.240-pH 7.0pH 6.820-Venous0-0.20106080Percent saturation

Hemoglobin is an allosteric protein. It facilitates the transport of oxygen and carbon dioxide in…

Answered: O, saturation curve is shown below for…

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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Calculate the percent oxygen saturation of myoglobin if 7 of 15 binding sites are occupied..
Give detailed Solution with explanation (no need Handwritten
What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.
5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 a Dсм 23 Torr Symbols: в Dсм 50 Torr x DCM I00 Torr o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Ka for O2 binding is defined for 0 and 100 Torr of dichloromethane For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of Kd Hb(O2)n Hb + nO2 % OXYGENATION
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…
e 1.0 0.5- 0 6. Answer the questions below about hemoglobin and myoglobin. a. Sketch and label the binding curves of Mb, Hb, and Hb below. pº₂ b. In the scenarios below for Hb, indicate what effect they would have on the binding curve and give a brief explanation? Scenario Decrease in the concentration of carbon dioxide (CO₂) Distal histidine (the histidine that aids in molecular oxygen binding) mutation to phenylalanine High heat and extreme pH changes Predict if the normal binding curve of Hb will shift right (Hbt), left (HbⓇ), completely to Mb, or no longer bind oxygen completely? Brief Explanation
Given the following, calculate Gk: ENa = +45 mV; Ek = -85 mV; ECl = -60 mV; GNa = 5x10-8 S; GCl =0; Vm = -70 mV
If normal plasma pH is 7.4 and normal [CO2) is 1.2 mM, what is the normal (HCO321? The pK9 for this system is 6.1. Phosphoric acid (H3PO4) has three dissociable protons, with the pK,'s shown below. Which form of phosphoric acid predominates in a solution at pH 4? Explain your answer. Acid H3POA 2.14 H2PO4 6.86 HPO,2- 12.4
. 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.
5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 Symbols: a Dсм 23 Torr • DCM 50 Torr x DCM I00 Torr o, 0 Torr DCM; О, 23 Torr DСМ Д, 50 Torr DСМ x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Kd for O2 binding is defined for 0 and 100 Torr of dichloromethane Kd Hb(O2)n nO2 Hb + Be sure to label the axes, indicate the units on both axes, and make the Hill plot so that the values of Kd are equivalent to those on the saturation plot above. Indicate whether cooperativity, as indicated by the Hill…
Below is a list of hypothetical Hemoglobin variants. Circle the name of the variant that is most likely to show an increase in BPG binding. Does such a hypothetical variant cause an increase or decrease in hemoglobin's affinity for oxygen? A. Hb Miami: Leu is substituted with Pro in an alpha helix B. Hb California: Val is substituted with Lys at pH 7.0 C. Hb New york: Tyr is substituted with Met, which disrupts the hydrogen bonding at the a131 interface. D All of the above
50 A 500 mL infusion of glucose 5% is being given at a rate of 167 mL/hr. How long will the infusion run at the specified rate?

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