Macmillan Learning Write the equilibrium-constant expression for the reaction A(s)+3 B(1)2C(aq) + D(aq) in terms of [A], [B], [C], and [D], as needed. Note that Kc, which is sometimes symbolized as Keq, denotes that the equilibrium constant is expressed using molar concentrations. For this question, K, means the same thing as Keq. K₁ = ICI²IDI Incorrect Answer Attempt 2

Macmillan Learning Write the equilibrium-constant expression for the reaction A(s)+3 B(1)2C(aq) + D(aq) in terms of [A], [B], [C], and [D], as needed. Note that Kc, which is sometimes symbolized as Keq, denotes that the equilibrium constant is expressed using molar concentrations. For this question, K, means the same thing as Keq. K₁ = ICI²IDI Incorrect Answer Attempt 2

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 17P

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Suppose the biochemical pathway represented in Equation 5-10a is coupled at its first step to the hydrolysis of ATP to ADP. How would this change the expres- sion for AG of the pathway?
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
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Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP = creatine + ATP at 37 °C, as it occurs in the cytosol of neurons, where [phosphocreatine] = 4.7 mM, [creatine] = 1.0 mM, [ADP] = 0.73 mM, and [ATP] = 2.6 mM. Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds Phosphorylated compound AGʻ° (kJ/mol) phosphoenolpyruvate -61.9 phosphocreatine -43.0 ADP (→ AMP + P;) -32.8 ATP (→ ADP + P;) -30.5
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The steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor (inhibitor A). The initial rate is given as a function ofsubstrate concentration in the following table: (a) What kind of inhibition (competitive, uncompetitive, or mixed) isinvolved?(b) Determine Vmax and KM in the absence and presence of inhibitor.
Calculate ΔG°′ for the reaction A + B ⇌ C + D at 25°C when the equilibrium concentrations are [A] = 10 μM, [B] = 15 μM, [C] = 3 μM, and [D] = 5 μM. Is the reaction exergonic or endergonic under standard conditions?
Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
14) Calculate K’eq and ΔG’0 for the following: A 0.1 M solution of glucose 1-phosphate at 25oC is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Glucose 1-phosphate (4.5 X 10-3 M) and Glucose 6-phosphate (9.6 X 10-2 M).
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Question 13 of 40 0% Identify the true characteristic of glutamate at its isoelectric point (pI). 00% The net charge of glutamate is positive. prrect The side chain of glutamate has a negative charge. L00% In an electric field, glutamate migrates toward the anode. orrect The net charge of glutamate is zero. 0% In an electric field, glutamate migrates toward the cathode. 0% Determine the pl of glutamate given its pK at each charge state. Give your answer to two decimal places. Progress Charge: 1+ 1- 2- 0% H,N- CHCO, CH, *H,N-CHCO,H *H,N-CHCO, *H,N–CHCO, CH, CH, pK = 9.67 CH, CH, pK = . = 4.25 0% pk = 2.19 CH, CH, CH, C=0 C=0 C=0 Ć=0 0% MacBook Pro Q Search Default Search &