17. Considering the following two reactionsAB AGº' = -23.5 KJ/molCD AG0¹ = +23.5 KJ/molWhich of the followings is correct for the reaction A + C → B + D?A. The reaction is at equilibriumB. The equilibrium constant equals 1.00C. Both A and BD. Neither A nor B18. Considering the shown reaction that occurs in the skeletal muscle, which of the following statementsis true?HOCH₂OHHAOHOHΑτρAPPCH₂0-℗KHOC. Both A and BD. Neither A nor BHHTOHOHBA. The only fate of the product B is to undergo glycolysisB. Accumulation of B would inhibit the reaction

∆G° is standard Gibbs free energy change. ∆G°' is the standard Gibbs free energy change under…

Answered: 17. Considering the following two…

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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3. Respiration is related to how cells balance redox reactions in the metabolic pathway. It can be aerobic if there is plenty of oxygen present or anaerobic if not. In class, we discussed the respiratory quotient for triolein as a carbon source. A. Calculate the respiratory quotient (RQ) for aerobic oxidation of the triglyceride formed by glycerin and three stearic acids (tristearin). Draw the structure and write the stoichiometrically balanced equation for the complete breakdown of the triglyceride by oxidation to CO₂ and water. B. As in part A, draw the structure of sucrose, write the stoichiometrically balanced equation and determine the RQ for it's metabolic breakdown to CO₂ and water. C. Anaerobic respiration occurs when cells operate without dissolved oxygen. List at least 4 different chemicals that act as electron acceptors when oxygen is not present.
Which of the following which of the following reactions is an endergonic reaction that could occur in a cell, but only if coupled to the hydrolysis of ATP? ( delta G= -32 kJ/ mol)?
4
3. Show the calculation of (1) the expected grams of alum (KAI(SO4)2 12 H2O) formed from the reaction of 1.4 grams of aluminum metal and then show the calculation of (2) the % yield if the actual yield of alum is 21.31 grams. Overall reaction is shown below: 2 Al + 2 KOH + 10 H2O + 4 H2SO4 →2 KAI(SO4)2 12 H2O + 3 H2(g)T
22. For the process, A B, Keq is 0.02 at 37°C. For the process, BC, Keq 1000 at 37°C. A. Determine Keq (AC), the equilibrium constant for the overall process A C, from Keq (AB) and Keq (BC). B. Determine standard-state free energy changes for all three processes and use AG'(AC) to determine Keq (AC). Make sure that this value agrees with that determined in part A of this problem.
1. Start with the Michaelis-Menten equation and convert it to a double-reciprocal equation. Show how you would make a linear Lineweaver-Burk plot using this equation. 2. Based on th chart make a Lineweaver-Burk plot and later use the plot to complete the information in the table.
Please calculate the ΔG of glucose transport into the cell if the concentration of glucose is 1mM inside the cell and 100μM outside. R=2cal/mol*K and T = 300K. A. 1.38kcal/mol B. -1.38kcal/mol C. 2.76kcal/mol D. -2.76kcal/mol
2. The Km of a particular enzyme is 2.0 x 105 M. If the initial velocity (Vo) is 0.16 mmol/min for [S] = 0.15 M, what will be the initial velocity when [S] =2.0 x 10+M?
4.2
1. A reaction in which a substrate is converted to a product is catalyzed by an enzyme. The reaction was determined to have ket = 10,000. s', KM = 90.0 µM, and a standard Gibbs free energy change of -13.8 kJ mol. Answer the following questions about experiments performed with 2.00 nM enzyme. R= 8.3145 J mol K. !3! a) Calculate the change in free energy for this reaction at room temperature (25.0°C) under the following conditions, and indicate whether the forward reaction is favored or not. i. [(S] = 2.00 µM and [P] = 2.00 nM. !! it. [S] = 2.00 uM and (P) = 2.00 uM.
6. An enzyme catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM/s. What is the reaction velocity when the substrate concentration is (a) 0.25 mM (b) 1.5 mM, and (c) 10 mM?
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM

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