Sketch the Hill plot for a system with negative cooperativity. Be sure to a) label your axes, and to indicate in your plot: b) the Hill constant, c) limiting slopes, d) Kd values and what binding site the Kd values correspond to.
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Sketch the Hill plot for a system with negative cooperativity. Be sure to a) label your axes, and to indicate in your plot: b) the Hill constant, c) limiting slopes, d) Kd values and what binding site the Kd values correspond to.
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- Calculate, or make a best estimate of, the unknown factors in the situations listed in Table 1. Table 1. Data for problem 1. To find Data (i) Ek [K+]out = 4 mM; [K+]in = 130 mM (ii) [Cl-]in [Cl-]out = 570 mM; ECl = -65 mV (iii) ECl [Cl-]out = 150 mM; [Cl-]in = 8 mM; in a mammal (iv) [Na+]in Overshoot of action potential = +35 mV; saline [Na+] = 112 mM (v) [K+]in Blood [K+] = 3.2 mM; undershoot of action potential = -87 mV (vi) ECa [Ca2+]out = 5.6 mM; free [Ca2+]in = 0.8 mM (vii) [K+]out [K+]in = 350 mM; Ek = -82 mV1) Explain chain-folded and spherulite structures. 2) A biomedical company is planning to design a robotic arm from polymeric biomaterials based on their stress-strain curves. You as a bioengineer/researcher in this company, are requested to choose the best material from different biomaterials (A, B, C, D, E, and F) based on their mechanical properties. Express your opinion shortly on the following questions? a) Difference between A and C? b) Difference between B and D? c) Difference between F and E? d) What would be your recommendation for the robotic arm? Why? Stress (MPa) 10.0 7.5 5.0 2.5 0.0 0 D Strain (%) 10 E F 15Give an interpretation for the following graph:
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- You have an initial solution in which you added quantities of “A” and “B” such that there is 4.5 M “A” and 2.5 M “B” and no complex (“AB”) at time 0. After equilibrium, you are able to isolate and quantitate the “AB” complex, and find its concentration is 1.5 M. Given that RT is 0.59 kcal/mol, what is the delta Go’ for the association reaction?An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value less than 1 b) should exhibit a sigmoidal binding curve c) should show a hyperbolic binding curve d) should give an nH value of 1 e) both a and b f) none of the above
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