(a) Interpretation: The enzyme that has the higher affinity for substrate should be determined. Concept introduction: Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate. E + S ⇌ k − 1 k 1 ES → k 2 E + P The rate of formation of product V 0 is given by Michaelis-Menten equation, V 0 = V max [ S ] [ S ] + K M The reaction rate when the enzyme is fully saturated with substrate is said to be V max . K M is the Michaelis constant which is the substrate concentration at the half of the V max .

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Answer 1

Question

Chapter 8, Problem 32P

Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + S⇌k−1k1 ES →k2 E + P

The rate of formation of product V₀ is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be V_max. K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

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a) What are the differences between the Direct & Indirect Immunofluorescence Assays? (0.5 mark) b) What are the advantages of the Indirect Immunofluorescence Assays? (0.5 mark) c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality? (2 marks)

a) What are the differences between the Direct & Indirect Immunofluorescence Assays? b) What are the advantages of the Indirect Immunofluorescence Assays? c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality?

Answer 2

Question

Chapter 8, Problem 32P

Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + S⇌k−1k1 ES →k2 E + P

The rate of formation of product V₀ is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be V_max. K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 3

Question

Chapter 8, Problem 32P

Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + S⇌k−1k1 ES →k2 E + P

The rate of formation of product V₀ is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be V_max. K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 8, Problem 32P

Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + S⇌k−1k1 ES →k2 E + P

The rate of formation of product V₀ is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be V_max. K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Expert Solution & Answer

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Check out a sample textbook solution

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Answer 5

Chapter 8, Problem 32P

Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + S⇌k−1k1 ES →k2 E + P

The rate of formation of product V₀ is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be V_max. K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Answer 6

Chapter 8, Problem 32P

Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + S⇌k−1k1 ES →k2 E + P

The rate of formation of product V₀ is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be V_max. K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Answer 7

Chapter 8, Problem 32P

Interpretation Introduction

(a)

Interpretation:

The enzyme that has the higher affinity for substrate should be determined.

Concept introduction:

Michaelis Menten model describes the kinetic properties of enzymes. Enzyme and substrate combines to form an enzyme-substrate complex and form a product or it can go back to dissociated enzyme and substrate.

E + S⇌k−1k1 ES →k2 E + P

The rate of formation of product V₀ is given by Michaelis-Menten equation,

V0=Vmax[S][S]+KM

The reaction rate when the enzyme is fully saturated with substrate is said to be V_max. K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Answer 8

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Answer 9

Interpretation Introduction

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

Answer 10

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Answer 11

Interpretation Introduction

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Answer 12

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Answer 13

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Answer 14

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Answer 15

Ch. 8 - Prob. 1P Ch. 8 - Prob. 2P Ch. 8 - Prob. 3P Ch. 8 - Prob. 4P Ch. 8 - Prob. 5P Ch. 8 - Prob. 6P Ch. 8 - Prob. 7P Ch. 8 - Prob. 8P Ch. 8 - Prob. 9P Ch. 8 - Prob. 10P

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(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Want to see the full answer?

Chapter 8 Solutions

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(b) Interpretation: The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration. Concept introduction: KM is the Michaelis constant which is the substrate concentration at the half of the Vmax.

(c) Interpretation: Enzyme that varies the equilibrium more in the product direction should be determined. Concept introduction: Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.

Want to see the full answer?

Chapter 8 Solutions

(b)

Interpretation:

The initial velocity of the reaction should be determined when catalyzed by the wild type enzyme at the 10 mM substrate concentration.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration at the half of the V_max.

(c)

Interpretation:

Enzyme that varies the equilibrium more in the product direction should be determined.

Concept introduction:

Enzymes act as catalysts which increase the rate of the reaction by lowering the activation energy. Most of the enzymes are proteins.