n 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?
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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?
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- The phosphoryl group transfer potentials for glucose-1-phosphate and glucose-6-phosphate are 20.9 kJ/mol and 13.8 kJ/mol, respectively. (a) What is the equilibrium constant for the reaction shown below at 25 °C? (b) If a mixture was prepared containing 1 m glucose-6-phosphate and 1 x 10-3 M glucose-1-phosphate, what would be the thermodynamically favored direction for the reaction?The ΔG°′ value for glucose-1-phosphate is -20.9 kJ/mol. If glucose and phosphate are both at 4.8 mM, what is the equilibrium concentration of glucose-1-phosphate?When a mixture of 3-phosphoglycerate and 2-phosphoglycerate is incubated at 25°C in the presence of the enzyme phosphoglycerate mutase (which catalyzes the intervconversion of the two substances) until equilibrium is reached, the final mixture contains 6 times as much 2-phosphoglycerate as 3-phosphoglycerate. Which of the following statements is most nearly correct when applied to the reaction shown below: 3-phosphoglycerate ------> 2-phosphoglycerate (R=8.315 J/mole.K) A. △G°' = +12.7 kJ/mole B. △G°' = 0 C. △G°' is incalculably large and positive D. △G°' = -4.44 kJ/mole E. △G°' cannot be calculated from the information gven
- What is the likely keq for an enzyme that has a deltaG =-18.3kj/mol?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.
- Determine the values of Km and Vmax for the decarboxylation of β-keto acid given the following data. Please show and label your plot. Show your calculations and box your final [S] in mol/l V in mM/ min 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256Given the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin at 25oC: ΔH° = –88 kJ/mol ΔS° = 0.3 kJ/mol. The free energy of hydrolysis of ATP in systems free of Mg2+ is −35.7 kJ/mol. When the concentration of this ion is 5 mM, ΔG°observed is approximately −31 kJ/mol at pH 7 and 38°C. Suggest a possible reason for this effect.Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following sets of data: a. Given [ Ca2+ ]0=1mM,[ Ca2+ ]i=100nM, find Eca2+ b. Given [ Cl- ]0=110mM,[ Cl- ]i=100mM, find Ecl
- 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?)The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy changeGiven that the standard free-energy change for the reaction glucose + Pi →glucose 6-phosphate is 13.8 kJ/mol, and the standard free-energy change forthe reaction ATP → ADP + Pi is −30.5 kJ/mol, what is the free-energychange for the reaction glucose + ATP → glucose 6-phosphate + ADP?