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Calculate the percent oxygen saturation of myoglobin if 7 of 15 binding sites are occupied..
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- Heart and muscle cells, where myoglobin resides, maintains an intracellular pO2 of about 2.5 torr. Calculate the fractional saturation (for human myoglobin) if a small change (1 torr) in oxygen partial pressure occurs in either direction (ie what happens at 1.5 torr, what happens at 3.5 torr?) and explain how a small change in oxygen pressure dramatically changes the myoglobin oxygen binding.A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?In active muscle cells, the pO2 is about 10 torr at the cell surface and 1 torr at the mitochondria(the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygentransported to the mitochondria of muscle cells by myoglobin (KD = 2 torr).
- In active muscle cells, the pO₂ is about 10 torr at the cell surface and 1 torr at the mitochondria (the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygen transported to the mitochondria of muscle cells by myoglobin (KD = 2 torr). A new oxygen transport protein that exhibits cooperative binding has been isolated and is being studied in the lab. Calculate the Ko value if Y = 0.76 when pO₂2 = 18 torr (assume n = 2.5). How does this compare to the K₂ value for hemoglobin? Does this protein bind more or less tightly to oxygen compared to hemoglobin?The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.From the figure of O2 binding to myoglobin and hemoglobin (ignore the linemarked as T) as described in lecture (shown below) answer the following questions. a) Estimate the P50 for myoglobin from the plot. Show how this estimation isdetermined from the binding curve above. ( The first ghraph) b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph) c)Using the binding curve on the previous page, show how you can estimate whatfraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value. If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increaseor decrease? Explain why this is so based on how this changes hemoglobin structure. If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at30 torr increase or decrease? Explain why this is so based on how this changes hemoglobinstructure.
- . Oxygen binding by the hemocyanin of the shrimp Callianassa has been measured. Using the following data, prepare a Hill plot and determine (a) Pso, (b) h (the Hill coefficient), and (c) the minimum number of oxygen binding sites on the protein molecule. Poz (mm Hg) Yoz Po, (mm Hg) Yo2 1.1 0.003 136.7 0.557 7.7 0.019 166.8 0.673 10.7 0.035 203.2 0.734 31.7 0.084 262.2 0.794 71.9 0.190 327.0 0.834 100.5 0.329 452.0 0.875 123.3 0.487 736.7 0.913Intracellular concentrations in resting muscle are as follows: fructose6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM;ADP, 0.5 mM; ATP, 5 mM; and Pi, 10 mM. Is the phosphofructokinasereaction in muscle more or less exergonic than under standard conditions?By how much?In a Myoglobin and azide ligand-receptor binding experiment, instead of using 3.5 µM myoglobin you used half of this (1.75 µM myoglobin), what would be that value of the Kd, that you calculated (how would the Kd change)?
- You have discovered a new form of mouse myoglobin that has a p50 of 9 Torr. At approximately what pO2 would this hemoglobin be 86% saturated with oxygen? 85 Torr 40 Torr 60 Torr 55 Torr Not enough information is given to answer this questionWhat 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.Myoglobin monomers are likely to have more hydrophilic amino acids on the protein surface than Hemoglobin monomers. True or False