(a) Interpretation: The results obtained with the mutant should be explained. Concept introduction: Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

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Answer 1

Question

Chapter 21, Problem 42P

Interpretation Introduction

(a)

Interpretation:

The results obtained with the mutant should be explained.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Interpretation Introduction

(b)

Interpretation:

The effect of substituting aspartic acid for serine should be predicted.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

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Select all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.

Answer 2

Question

Chapter 21, Problem 42P

Interpretation Introduction

(a)

Interpretation:

The results obtained with the mutant should be explained.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Interpretation Introduction

(b)

Interpretation:

The effect of substituting aspartic acid for serine should be predicted.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

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Answer 3

Question

Chapter 21, Problem 42P

Interpretation Introduction

(a)

Interpretation:

The results obtained with the mutant should be explained.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Interpretation Introduction

(b)

Interpretation:

The effect of substituting aspartic acid for serine should be predicted.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

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Answer 4

Question

Chapter 21, Problem 42P

Interpretation Introduction

(a)

Interpretation:

The results obtained with the mutant should be explained.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Interpretation Introduction

(b)

Interpretation:

The effect of substituting aspartic acid for serine should be predicted.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

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Answer 5

Chapter 21, Problem 42P

Interpretation Introduction

(a)

Interpretation:

The results obtained with the mutant should be explained.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Interpretation Introduction

(b)

Interpretation:

The effect of substituting aspartic acid for serine should be predicted.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Answer 6

Chapter 21, Problem 42P

Interpretation Introduction

(a)

Interpretation:

The results obtained with the mutant should be explained.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Answer 7

Chapter 21, Problem 42P

Interpretation Introduction

(a)

Interpretation:

The results obtained with the mutant should be explained.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Answer 8

Interpretation Introduction

(b)

Interpretation:

The effect of substituting aspartic acid for serine should be predicted.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Answer 9

Interpretation Introduction

(b)

Interpretation:

The effect of substituting aspartic acid for serine should be predicted.

Concept introduction:

Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.

Answer 10

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Answer 11

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Answer 12

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Answer 13

Ch. 21 - Prob. 1P Ch. 21 - Prob. 2P Ch. 21 - Prob. 3P Ch. 21 - Prob. 4P Ch. 21 - Prob. 5P Ch. 21 - Prob. 6P Ch. 21 - Prob. 7P Ch. 21 - Prob. 8P Ch. 21 - Prob. 9P Ch. 21 - Prob. 10P

Solution Summary: The author explains that Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-

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Chapter 21 Solutions