Which of the following is incorrect about the Michaelis-Menten plot?a. The y-axis is velocity and the x-axis is [substrate]b.It is based on E + S to reversibly form ES and then this to form E + PO c. The data is plotted using the Michaelis-Menten equationOd. It has a sigmoidal shape

Michaelis–Menten saturation curve for an enzyme reaction following the Michaelis-Menten kinetic…

Answered: Which of the following is incorrect…

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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Write C if only statement A is correct, H if only statement B is correct, E if both statements are correct, M if both statements are incorrect. (A) For the Lineweaver-Burk plot, the slope of the line reflects the ratio between the maximum velocity and the Michaelis constant. (B) Meanwhile, the y-intercept is the maximum velocity.
For the following problem indicate the values for each part of the equation and solve for the unknownvalue:Peter adds 200 μL of bacteria to a tube containing 2 mLs of nutrient broth and then adds 300 μL of acertain disinfectant. The final concentration of the disinfectant in this tube after adding it is 5%.C1=C2=V1=V2=
SUBSTRATE CONCENTRATION [S] µM INITIAL VELOCITY V0 s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 (i) a) Construct an empty table with the following column headings: Substrate concentration [S] and initial velocity (Vi) where [S] has the unit µM, and Vi has the unit mM/s. (ii) The table provided is the enzyme kinetic data for your mutated enzyme, whereby Vi was expressed using the unit ∆A(405 nm)/s. Using the standard curve, express Vi with the unit mM/s rather than ∆A(405 nm)/s. Place your answer in the table above alongside the appropriate [S]. Hint: To answer this question you need to use this standard curve equation=0.0419x (The slope of the line is= 0.0419) (iii) The unmutated form of your protein has a Km of 25 µM and a Vmax of 43 mM/s. The enzyme kinetic data for your enzyme with the amino acid substitution should now be displayed in the table above. Based on these data, what is Vmax? Km? and…
Suppose you wish to sediment a sample of spherical protein molecules (molar mass of 98.1 kg/mol and radius 3.40x10-9 m) in a liquid using a centrifuge. The sample is placed 5.0 cm from the centrifuge's axis of rotation and is rotated at 6000 Hz. a) What is the centripetal acceleration (i.e. the "g") the sample experiences from the centrifuge? b) If the liquid has a density of 900 kg/m3 and the terminal velocity of the protein is 4.10x10 6 m/s, what is the viscosity of the liquid?
You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
You want to prepare 500 mL of the macronutrient and micronutrient stock solutions which have 100X and 1000X higher concentration, respectively, than the required concentration in the culture mediuma)If 0.17 g/L KH2PO4 is required in MS medium, determine the mass (g) of KH2PO4 that is required to prepare the stock solution and the volume required (mL) to prepare 200 mL MS medium. Show your work.
o NB4: Why do you think you first had to make the 1 mM solution instead of working directly from the stock solution?
What is the optimal substrate concentration for the enzymatic reaction presented in the Lineweaver-Burk plot below? a. -0.3211 units/mL b. –3.114 units/mL c. None of these values represent the optimal substrate concentration shown in the Lineweaver-Burk plot d. 3.114 units/mL e. 0.3211 units/mL
I have a question, what are these ''a'' means in this plot? Normally its 1/vmax or -1/km. Please be specific. Thank you.
Using C1*V1 = C2*V2, please complete the calculations for the substrate row & show me how to do it as I am unsure. *The final sample is contained in using 2mL centrifuge tubes. answer all or else I will upvote
List the 6 assumptions by Henri and Michaelis-Menten in describing the relationship between initial velocity and substrate concentration versus the Briggs-Haldene modifications of the Michaelis-Menten equation
In a typical enzyme-catalyzed reaction, what are the relative concentrations of reactants and products as compared to the enzyme concentration?

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Which of the following is incorrect about the Michaelis-Menten plot? a. The y-axis is velocity and the x-axis is [substrate] Ob. It is based on E + S to reversibly form ES and then this to form E + P C. The data is plotted using the Michaelis-Menten equation Od. It has a sigmoidal shape