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- Bohr for me, not for thee. Does myoglobin exhibit a Bohr effect? Why or why not?Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.A 0.0284 M aqueous solution of lactic acid, HC3H5O3, a substance that accumulates in the blood and muscles during physical activity, is found to be 6.7% ionized. Determine the value of Ka for lactic acid.
- 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.If instead of using 3.5 µM myoglobin (receptor) you used half of this (that is, 1.75 µM myoglobin), what would be that value of the Kd, that you calculated ( how would it change)? Please explain so I can solve on my own :) (How does changing concentration of the receptor in a ligand-receptor binding experiment affect the dissociation constant?)In a rat cardiomyocyte, the levels of creatine, phosphocreatine, and free phosphate were found to be 37.6mM, 40.3mM, and 8.02mM, respectively. Given that the standard free energy change is –43.0 kJ/mol, what is the true free energy change for phosphocreatine hydrolysis in the cardiomyocyte described above?
- 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.1. a. 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). b. 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?2.For question number 1 if a mixture was prepared containing 1 M Glucose 6-Phosphate and 0.001 M Glucose 1-Phosphate the ∆G for this reaction is: included question 1 however, need help with 2 and provided the option for the answer 1.What is the Keq for the conversion of Glucose 1-Phosphate to Glucose 6-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are 20.9 kJ/mol and 13.8 kJ/mol respectively?
- When you hold a weight at arm's length, you are not doing any thermodynamic work but the muscles supporting the weight are nevertheless consuming energy. Describe, on the molecular level, how muscles might maintain such state of constant tension without contracting. Why does this state consume ATP?The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.During movement, muscle cells require large amounts of ATP to fuel their contractile apparatus. These cells contain high levels of creatine phosphate (Figure Q13–11), which has a standard free-energy change (ΔG°) for hydrolysis of its phosphate bond of –10.3 kcal/mole. why is this a useful compound to store energy?