Assume you were assigned to use NMM (N-methyl-morpholine) to synthesize dipeptide 3 following the procedure described in Experiment Part II. The amount of NMM you will have to measure for your reaction is 275 mg 275 microliters 2.75 microliters 253 mg
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- The enzyme urease increases the rate of urea hydrolysis at pH 8.0 and 20 °C by a factor of 1014. Suppose that a given quantity of urease can completely hydrolyze a given quantity of urea in 19 minutes at pH 8.0 and 20 °C. How long would it take for this amount of urea to be hydrolyzed in the absence of urease at the same temperature and pH in sterile conditions? Include two significant figures in your answer. timeuncatalyzed years * TOOLS x10What is the turnover number in molecules/min of a catalase enzyme molecule that cleaves 8.4 x 107 H₂O₂ molecules in 15 minutes?For this question you will need to work all of your answers on scratch paper. Once completed, upload an image of your answers showing all work and clearly identifying your answers. Use the Browse My Computer button to upload an image. It is known that the activity of penicillin declines over several weeks when it is stored at room temperature in the absence of stabilizers. The following concentrations of active penicillin was found as several weeks passed. This data shows the decline in effectiveness of the penicillin due to a decomposition reaction. Time in weeks 0 5.0 10.0 15.0 20.0 25.0 30.0 Concentration of Penicillin in Molarity 0.076 0.046 0.020 0.010 0.0050 0.0020 0.0010 a. Show all your work, what is the average rate of the reaction? b. Show all your work, what is the instantaneous rate from 5.0 to 20.0 weeks? c. Show all your work, what is the instantaneous rate from 0.0 to 10.0 weeks? d. Show all your work, what is the instantaneous rate from 15.0 to 30.0 weeks?
- A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction The researchers begin to characterize the enzyme. a)In the first experiment, with [Et] at 4 nM, they find that the Vmax is 1.6 μM s-1. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) b)In another experiment, with [Et] at 1 nM and [HAPPY] at 30 μM, the researchers find that V0300 nM s-1. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) c)Further research shows that the purified happyase* used in the first two experiments wasactually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax in (a) is increased to 4.8 μM s-1, and the measured Km in (b) is now 15 μM. For the inhibitor ANGER, calculate the values of αand α’.Write and discuss the mechanism of the reaction that happens at the active site of the enzyme cathecol oxidase.Describe the adsorption mechanism of this inhibitor molecule on mild steel?
- Calculate the velocity of the reaction (M · s–1) of an α-amino group in a blood protein at 37°C if its concentration is 0.60 mM and the partial pressure of carbon dioxide is 40 torr. Use 2 significant figures and scientific notation (example: 1000 would be entered as 1.0e+3). The rate constant k for this reaction is 4950 M–1·s–1.A research group discovers a neW version oI happyasee, which they nappyase", that catalyzes the chemical reaction HAPPY = SAD The researchers begin to characterize the enzyme. In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat for happyase*? kcat 400 S In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i the measured Km of happyase* for its substrate HAPPY? Km 10 x10–6 Incorrect Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM. S For the inhibitor ANGER, calculate the values of a' and a. a' 2 Incorrect 2The hydrolysis of carbobenzoxyglycyle-L- tryptophan catalyzed by the pancreatic carboxypeptidase was carried out according to the following equation. Carbobenzoxyglycyle- L- tryptophan + H20 → carbobenzoxyglycyine +L- tryptophan The data below represent the rate of formation of L tryptophan at pH = 7.5 ,25°C. The results are listed as follows: 20.0 IS] (mM) 2.5 5.0 10.0 15.0 Rate(mMs" 0.024 0.053 0.060 0.064
- The acid-catalyzed hydrolysis of sucrose, C12H22O11 + H₂O + H+ -> C6H12O6 + C6H12O6 + H+ is known as "inversion of sucrose" because the angle, a, by which the solution rotates polarized light changes from positive to negative as the reaction proceeds (data from 30 degree C): t/hr a 0 78 2 71 4 12 18 24 42 65.10 44.60 32.40 22.45 2.30 48 -1.96 61 -9 86 95 -15.80 -17.25 -21.15 ∞ Use this data to show that the reaction is first order and determine its rate coefficient (at 30 degree C).Coenzyme F430 is a nickel-containing tetrapyrrole that is required by methyl-coenzyme M reductase. It is one of a class of nickel chlorins found in nature. Each molecule of cofactor 430 contains 1 atom of nickel. By mass, nickel is 6.47 % of the molecular formula. What is the molar mass of Coenzyme F430?Temperature effect on the degradation of a multisulfa preparation was evaluated at 60 and 70 C. If the first-order reaction rate constants responsible for the degradation at these two temperatures were 8.2 x 10-4 and 1.96 x 10-3 hr-1, respectively, answer the following TWO questions. 6. Calculate the activation energy, Ea, for this drug in this temperature range (in kcal/mol). (The gas constant; R = 1.987 cal/deg mol) ln (k2/k1) = Ea/R (T2 – T1) / (T2 x T1) ln (0.00196/0.00082) = Ea/1.987 (343 – 333) / (343 x 333) Ea = 19,777 cal/mol ~19.8 kcal/mol The teachers work in in bold, can you explain how to solve as it?