3) For Run 1, which reaction was closest to 100% yield? For Run 2, which reaction was closest to 100% yield? DATARecord all masses to the maximum number ofRun 1Run 2sig figs200°C400°C1.Mass of beaker81.06127.9862.Mass of beaker + NaHCO385.45732.2673.Initial mass of NaHCO34.4764.292Mass of beaker plus products afterheating.4.84.3 8030.7425.Mass of product (actual yield)There are three theoretically possible chemical reactions that could occur during the thermal decomposition of bakingsoda.1)sodium bicarbonate (s) → sodium hydroxide (s) + carbon dioxide (g)2)sodium bicarbonate (s) → sodium oxide (s) + carbon dioxide (g) + water (g)3)sodium bicarbonate (s)→ sodium carbonate (s) + carbon dioxide (g) + water (g)

The percent yield is the actual yield divided by the theoretical yield. It is determined by dividing…

Answered: 3) For Run 1, which reaction was…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Considering PNPP → PNP reaction, would you expect to see more intense or pale color for the reaction that contain the inhibitor? Explain.
Consider the analogy of the jiggling box containing coins that was described on page 85. The reaction, the flipping of coins that either face heads up (h) or tails up (T), is described by the equation h ↔ T, where the rate of the forward reaction equals the rate of the reverse reaction.a. What are ΔG and ΔG° in this analogy? b. What corresponds to the temperature at which the reaction proceeds? What corresponds to the activation energy of the reaction? assume you have an “enzyme,” called jigglase, which catalyzes this reaction. What would the effect of jigglase be and what, mechanically, might jigglase do in this analogy?
Find kcat for a reaction in which Vmax is 4 × 10-4 mol-min-1 and the reaction mixture contains one nanogram of enzyme. The molecular weight of the enzyme is 200,000 Da (1 Da = 1 g/mol). 2 x 10-13 min-1 2 x 10-11 min-¹ 80 min-¹ 8 x 107 min-¹ 8 x 10¹0 min-¹
From a kinetics experiment, kcat was determined to be 295sec-1. For the kinetic assay, 0.3mL of a 0.25mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 3mL. Calculate Vmax (µM∙min-1) for the enzyme and catalytic efficiency ( in M-1sec-1) for the enzyme. The Km for the enzyme was determined to be 2.55 x 10-2M.
You run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S concentrations. What is the Km (in mM) for Enzyme A?
A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction: HAPPY-SAD The researchers begin to characterize the enzyme. The researchers determined the kcat of the enzyme to be 452 s-1. In a separate experiment with [E;) at 1.5 nM and [HAPPY) at 38 µM, the researchers find that Vo is equal to 320 nM s-1. What is the measured Km of happyase* for its substrate HAPPY? Make sure to include units in the answer.
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
For an enzyme that has a Km of 25 mM, Vmax of 50 mM/s and kcat of 250 s-1, how long does a single reaction take? Select one: 50 ms 250 ms 4 ms 25 s 4 s
If protein X produces a higher absorbance reading at pH 7 than it does at pH 9, what can you conclude? Question 1 options: A lesser amount of protein X was used in the reaction at pH 7 than at pH 9. A greater amount of protein X was used in the reaction at pH 9 than at pH 7. Protein X is a more efficient catalyst at pH 7 than it is at pH 9. Protein X is a more efficient catalyst at pH 9 than it is at pH 7.
The IAP kinetics assay was preformed at a basic pH. What does this tell you about the reaction environment ?
Where do lines intersect on a Lineweaver-Burk plot showing competitive inhibition? Uncompetitive inhibition? Noncompetitive inhibition? 4.
Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve?

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