Describe how you would make the following solution containing two enzymes. 1 mL total volume in Buffer X with 10nM of enzyme A and 50nM of enzyme B You are given a solution of enzyme A at 1 mg/mL and a solution of enzyme B at 1 mg/mL. The molecular weight of enzyme A is 75,000 g/mol and the molecular weight of enzyme B is 130,000 g/mol.
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Describe how you would make the following solution containing two enzymes.
1 mL total volume in Buffer X with 10nM of enzyme A and 50nM of enzyme B
You are given a solution of enzyme A at 1 mg/mL and a solution of enzyme B at
1 mg/mL. The molecular weight of enzyme A is 75,000 g/mol and the molecular weight of enzyme B is 130,000 g/mol.
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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?As an intermediate step in making the enzyme solution, you need to prepare Buffer X using the stock solutions of each chemical. Describe how you would make 100 mL of buffer X that has the following concentrations and pH: 50mM NaCl, 20mM Tris, 5mM MgCl2, pH 7.5 You do this starting with stock solutions of 1M NaCl, 1M Tris, 1M MgCl2, and water and a pH meter.Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD what are the reactants and what are the products is this reaction spontaneous? How do you know? Is energy released or consumed by this reaction? If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneous
- This is a plot under standard conditions of free energy corresponding to a chemical reaction of A+B to C+D. What will happen if only C+D are present under standard temperature and pressure? Please explain why.Given the following enzyme kinetics data, determine the maximal velocity and the Michaelis constant of the enzyme. Show your solutionsAn enzyme (molecular weight= 24 kDa, pI= 5.5) is contaminated with two other proteins, one witha similar molecular mass and a pI of 7.0 while the other has a molecular mass of 100 kDa and a pIof 5.4. Suggest how the contaminated enzyme can be purified.
- Find kcat for a reaction in which Vmax is 4 × 10-4 mol•min-1 and the reaction mixture contains one microgram of enzyme (the molecular weight of the enzyme is 200,000 D). Show your work/reasoning.Why can’t an enzyme have a kcat/KM value greater than 109 M−1 ∙ s−1?For the series of reactions below, what is the overall reaction and the value of ∆Go’(kJ/mol) for this set of reactions? Is the reaction spontaneous? (1) 2 Pi+ H2O ➔Pyrophosphate+ H2O (with 5 mM Mg2+) (2) (Mg)Pyrophosphate + AMP ➔(Mg)ATP (3) (Mg)ATP + creatine ➔creatine-phosphate + (Mg)ADP
- For the following reaction, 4.91 grams of water are mixed with excess chlorine gas. The reaction yields 12.5 grams of hydrochloric acid.chlorine (g) + water (l) hydrochloric acid (aq) + chloric acid (HClO3) (aq) What is the theoretical yield of hydrochloric acid ? grams What is the percent yield of hydrochloric acid ? %A sample of hydrogen peroxide solution has a mass of 4.599 g. After reacting with the enzyme solution, the moles of oxygen are 0.00284 moles. What is the percent hydrogen peroxide in the solution?Given the following information about an enzymatic reaction, calculate the initial velocity. Your numerical answer is assumed to have the units of nM sec-1. Vmax = 5 nM sec-1 KM = 1 mM [S] = 0.25 mM