Which of the above curves corresponds to myoglobin in a solution containing physiological concentrations of CO2 and BPG at a pH of 6.8? O O O O Saturation (Y) Curve 1 Curve 2 T Curve 3 Curve 4 None of the above 3 4 po2
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- 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 EclHeart 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.Carbon monoxide binds the heme of hemoglobin in the same position as O2; however, it binnds 200 times better than 02 If we use a value of 40 torr for hemoglobin's Pso for 0z. what is its P5o for CO? 0.05 torr 0.20 torr 5 torr 200 torr O 8,000 torr
- The E1% at 280 nm of the protein myosin is 0.842. You take 40µl of a myosin solution of unknown concentration and add water to a final volume of 2.0 ml. The absorbance of this solution at 280 nm is 0.771. What is the concentration of the undiluted myosin solution? (units = mg/ml).calculate the actual free energy of hydrolysis of ATP, delta Gp in the erythrocytes of a new species. The standard free-energy of hydrolysis of ATP is also -30.5kJ/mol in this species, but the concentrations in this specie's erythrocytes are 0.00775 mM ATP, 0.00027 mM ADP and 0.00418 mM Pi. Assume the pH is 7.0 and the body temperature of this species is 43.0oC. Calculate your answer as kJ/mol to two decimal places.1 Gren: molanty of CsP stlutan -010M = 0.10mol/L vdm me of SoutoL molar mass of csp= 249.68 g/ mole %3D moles af CSP = molahty of CSPX volume of shreoon mdes of asp = 0.10 mol/xIL moles of cSp: 0-10 mol mass of csP-moles of CSPXmolar mass of CsP = 0.10mol X249.c689/mde mass of CSP= 24.9689
- 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).Derivatioh The equilibrium between dissolved CO2 and carbonic acid can be represented by k12 H+ + HCO3 H2CO3 k21 k13 || k31 К23 К 32 CO2 H2O Show that k23 d[CO2] = (k31 + k32)[CO2] - (k13 + 3 )tH* I[HCO3¯1 K dt where K = [H+][HCO3¯]/[H2CO3]. Step 1 of 4 The equilibrium between dissolved CO2 and carbonic acid can be represented by k12 H+ + HCO; H,CO3 k21 k13 k31 k23 К 32 CO2 H2O d[CO2] corresponding to the given equilibrium. (Assume that H2O is incorporated in the appropriate equilibrium constants. Use the following as necessary: [CO2], [H+], Give the expression for dt [HCO3 ], [H2C03], k12, k13, k21, k23, k31, and k32-) k23 H HCO3 d[CO2] (k31 + k32)[ CO2] - (kK13 + k dt SubmitA 100 ml of a 1% sol'n of boric acid (freezing point = -0.29) isotonic w/ blood by NaCl (freezing point = -0.58). what grams is needed to make it an isotonic? what weight of NaCl is needed to a 2% sol'n of atropine sulfate (E=0.13) made isotonic with blood plasma?
- 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?Which of the equations below best represents how excess acid in the blood plasma can be removed in the lungs by breathing? H+ (aq) + 0. 2(g) OH + H₂ CO (aq) OH+ + O (aq) 2(g) → H, CO. H + O₂ (aq) 2(g) 3(aq) 3(aq) → H₂O(g) + CO2(g) + CO2(g) → H₂O H, CO3(aq) → HCO, OH t + HCO3(aq) → H₂ CO3(g) → H₂O(g) (aq) → H, CO3(aq) 3 (aq) + CO2(g) H₂O(g) + CO2(g)An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds toa second, related protein, it forms three fewer hydrogenbonds, reducing its binding affinity by 11.9 kJ/mole. Whatis the K for its binding to the second protein? (Free-energychange is related to the equilibrium constant by the equa-tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)and T is 310 K.)
