The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined. Concept Introduction: Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides. These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline. Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

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Answer 1

Question

Chapter 19.11, Problem 19.18Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides.

These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline.

Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.

Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

(b)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

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Answer 2

Question

Chapter 19.11, Problem 19.18Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides.

These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline.

Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.

Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

(b)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

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Answer 3

Question

Chapter 19.11, Problem 19.18Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides.

These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline.

Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.

Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

(b)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

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Answer 4

Question

Chapter 19.11, Problem 19.18Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides.

These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline.

Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.

Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

(b)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

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Answer 5

Chapter 19.11, Problem 19.18Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides.

These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline.

Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.

Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

(b)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

Answer 6

Chapter 19.11, Problem 19.18Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides.

These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline.

Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.

Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

Answer 7

Chapter 19.11, Problem 19.18Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide trp-val-gly and bond of peptide trp-val-gly that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Certain enzymes called proteolytic enzymes are involved in cleavage of the peptide bonds that are found in the primary structure of polypeptides.

These proteolytic enzymes are often refereed as serine proteases because of the presence of a nucleophilic serine at the active site of the enzyme. The proteolytic enzymes are classified on the basis of the specificity of enzyme. For example, the trypsin proteases cleave specifically at the carbonyl end of positively charged amino acids such as arginine or lysine except for the cases of amino acid that are followed by amino acid proline.

Chymotrypsin cleaves at the carbonyl terminal of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.

Elastase cleaves at the C-terminus of valine, serine, alanine, leucine, glycine, or isoleucine.

Answer 8

(b)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

Answer 9

(b)

Interpretation Introduction

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

Answer 10

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Answer 11

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Answer 12

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Answer 13

Ch. 19.8 - Prob. 19.12Q Ch. 19.10 - Prob. 19.13Q Ch. 19.10 - Prob. 19.14Q Ch. 19.10 - Prob. 19.15Q Ch. 19.10 - Prob. 19.16Q Ch. 19.11 - Prob. 19.17Q Ch. 19.11 - Prob. 19.18Q Ch. 19.11 - Prob. 19.19Q Ch. 19.11 - Prob. 19.20Q Ch. 19 - Prob. 19.21QP

Concept explainers

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Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).

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Chapter 19 Solutions

Concept explainers

Videos

Interpretation: The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined. Concept Introduction: Refer to part (a).

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Chapter 19 Solutions

Interpretation:

The structural formula of the given peptide phe-ala-pro and bond of peptide phe-ala-pro that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).