chSelect all statements that are correct. Note there might be more than 1 correctstatement.From the Lineweaver-Burk plot the equilibrium constant (Keq) can be obtainedThe Lineweaver-Burk plot gives a more accurate prediction for Vmax than the Michaelis-Menten plotThe Lineweaver-Burk plot assumes that products and reactants are present at equalconcentrations during the entire time of the reactionThe Lineweaver-Burk plot shows velocity of reaction vs substrate concentrationThe Lineweaver-Burk plot shows 1/velocity of reaction vs 1/substrate concentrationO20°CD)//E

The Lineweaver -Burk plot shows velocity of reaction vs substrate concentration. The Lineweaver…

Answered: Select all statements that are correct.…

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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The concept of determining which reactant is limiting and which is in excess is akin to determining the number of sandwiches that can be made from a set number of ingredients. Assuming that a cheese sandwich consists of 2 slices of bread and 3 slices of cheese, determine the number of whole cheese sandwiches that can be prepared from 36 slices of bread and 51 slices of cheese.
(please type answer fast).
1) Define metabolism and describe the importance of metabolism to life. 2) Calculate the change in free energy (∆G ) for the below reaction and answer the two follow up questions: Gfinal state = 3.4 kcal/ mol and Ginitial state = 10.7 kcal/ mol Recall: ∆G = Gfinal state – Ginitial state a. Is this a spontaneous or non-spontaneous reaction? Explain. b. Is there energy released from this reaction which can be used to do work? Explain. 2) List four conditions which impact an enzymes rate of activity. Explain.
The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)
Draw Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Vmax values for the inhibited and uninhibited rxns? Is the inhibitor competitive or noncompetitive? [S] (M) 10,000 1 x 104 2.000-5 x 104 666673 1.5 x 10-3 400- 2.5 x 10-³ 2005x103 V, No Inhibitor (Arbitrary units) 0.026 38,461 0.092 10.87 37100 0.136 7.35 Wak 0.150 -67 0.165 6.06 L slope: 0033 yint=5057 полесте um.x=0.198 km 6.5x 10-4 0.010 0.040 25 10.086 11.63 0.120 8.33 0.142 7.04 2500 V, Inhibitor Present (Arbitrary Units) 100 ↓ $op.= .009 yint: 5.21 900x12 km: 1.73 y/o conf. V10-3 321000
make a Gibbs free energy graph as free energy as y-axis a for the transition state as a function of [Gdn HCl] (x-axis) with a line of best fit
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released Energy

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