In the absence of 2,3-bisphosphoglycerate, the binding of oxygen by hemoglobin: a. is characterized by cooperativity b. resembles that of myoglobin c. binds at the end of the hemoglobin molecule d. is stabilized as the deoxy confor
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- Which of the following statements about the I state of hemoglobin is FALSE? a, iron ion is pulled to the plane of the heme ring b. stabilized by ion pairing at the dimers interface c. 2,3-bisphosphoglycerate shifts the RT equilibrium towards the T state O d. tense state of hemoglobinA The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding oxygen to hemoglobin would be altered by the change in conditions noted. 2. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 poz pO2Which statement is true for the heme group present myoglobin: a. Oxygen binding to heme group is influenced by serine residues within proteins’ sequences. b. Oxygen binding to heme can become irreversible as a result of interaction with certain protein residues. c. Oxygen reversibly binds to the heme prostetic group and this binding is influenced by histidine residues within the myoglobin sequence. d. The heme group dissociates from Mb after oxygen is released.
- Explain how the binding of molecular oxygen (O2) to haemoglobin affects the tertiary structures of each monomer. Hence, explain how this influences the quaternary structure of the haemoglobin molecule, and how this helps haemoglobin to transport O2 from the lungs to the muscles.d) Determine which statements apply to hemoglobin, myoglobin, or neither (you can write in the corresponding numbers for each statement, as appropriate) Hemoglobin Myoglobin Neither 1. Oxygen binds irreversibly to this molecule.2. This molecule has greater affinity for oxygen.3. The oxygen dissociation curve is sigmoidal in shape.4. Carbon monoxide binds at an allosteric site, lowering oxygen binding affinity.5. The binding pattern for this molecule is considered cooperative.6. This molecule delivers oxygen more efficiently to tissues.7. As oxygen binds to this molecule, the shape of the molecule changes, enhancing further oxygen binding.8. The oxygen dissociation curve is hyperbolic in shape.Compare the structure and function of hemoglobin and myoglobin. Which oxygen binding curve in the graph below belongs to myoglobin and which to hemoglobin? Please specify. Explain the effect of pH on oxygen binding to hemoglobin, and show on the graph in which direction the pH will shift if it falls below the physiological pH value (7.4).
- Which of the following is incorrect about 2,3-bisphosphoglycerate (BPG)? It is highly (-) charged b. It prevents binding of O₂ to hemoglobin Oc. It binds only to the relaxed (oxy) conformation of hemoglobin Od. It binds in the space between the four subunits of hemoglobin a.After spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?Write the reversible equation that shows the reaction of hemoglobin (Hb) with: A. Oxygen B. Carbon dioxide
- a.What is the difference between the 5th and 6 coordination sites in the heme group? b.What is the change of the oxygen dissociation curve represented by hemoglobin before and after dissociation into subunits? Briefly explain why.Which of the following is true about the T (tense) -->R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O2 to a subunit T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between b subunits than does the R state. D. When hemoglobin undergoes the T--> R transition, the structures of the individual subunits change dramatically.In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.