30. assicuatuib if 2alpha and 2 beta chains to form adult hemoglobin
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30. assicuatuib if 2alpha and 2 beta chains to form adult hemoglobin
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- You know that the main function of RBCs is to carry O2 from lungs to tissues. Please kindly discuss this function at the molecular level (at the level of hemoglobin structure α & β chains) taking in consideration 2, 3-BPG.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 saturationpO2 in tissues p02 in lungs 1.00 Oxygen-binding curves for normal Normal Hb hemoglobin, 50% carboxyhemoglobin, and hemoglobin from 0.8 an anemic individual. 0.6 Y 50% COHB 0.4- Anemic individual 0.2 4 8 12 pO2 (kPa) Box 5-1 Figure 2 Lehninger Principles of Biochemistry, Seventh Edition O 2017 W. H. Freeman and Company r aye i UIE I. Answer the following questions. Do not forget the units. 1) From the binding curve for normal Hb shown above, what is the Ka of normal hemoglobin?
- Figure 5 shows oxyhemoglobin dissociatlon curves at pH 7.2 and pH 7.4. Which of the following is true at PO2 less than 40 mm Hg? 27. % saturation af haemogiobin 100 pH 7.4 80 60 pH 7.2 40 + 20 10 20 30 40 50 60 70 Po; (mm Hg) Figure 5 A. Hemoglobin retains less O2 at pH 7.4 compared to pH 7.2. B. Hemoglobin retains less O2 at pH 7.2 compared to pH 7.4. C. The release of O2 from hemoglobin is not influenced by the production of CO2. D. At pH 7.2 where CO2 production is less than pH 7.4, hemoglobin releases less O2.{1q}. 1. Why is cyanmethemoglobin method preferred than other methods? 2. In what circumstances is the copper sulfate method used? 3. Discuss the synthesis and breakdown of hemoglobin.?A patient has thalassemia, a genetic disorder characterized by abnormal synthesis of globin proteins and excessive destruction of erythrocytes. This patient is jaundiced and is found to have an excessive level of bilirubin in his blood. Explain the connection.
- A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?2. 3. 4 6. In this image, the bacteria in circles 1 and 4 is demonstrating: presence of catalase • presence of coagulase O absence of catalase O absence of coagulase presence of hydrogen peroxide absence of hydrogen peroxide presence of antibodies absence of antibodies IcstSketch out the binding site of Hemoglobin with oxygen bound . ( You can abstract the Heme ring out i.e. not draw each chemical bond). Please label both imported HIS residues.
- Which of the following are true of normal adult hemoglobin? Choice 1 of 4:can bind four Fe2+ ions Choice 2 of 4:can covalently bind four O2 molecules Choice 3 of 4:can adopt 2 different conformations, with different orientations of αβ dimers Choice 4 of 4:can bind four BPG molecules to stabilize the T stateBelow is the O2 binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). A Hb 20 40 60 80 100 pO2 (torr) a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [ Select ] b. Which curve has the lowest affinity (as measured by the p5o)? [ Select ] c. Which curve lacks cooperativity? [ Select ] Fraction of Hb bound with Oxygen 0.2 0.4 0.6 0.8 0'0 >Hemoglobin has a ________ binding affinity at pO2 = 20 Torr and pO2 = 100 Ťorr. Low; High High; High High; Low Low; Low A B TANA AHAN Home stip FOR 120 binding affinity at
