The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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 19.19Q

Interpretation Introduction

Interpretation:

The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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 2

Question

Chapter 19.11, Problem 19.19Q

Interpretation Introduction

Interpretation:

The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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 3

Question

Chapter 19.11, Problem 19.19Q

Interpretation Introduction

Interpretation:

The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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 4

Question

Chapter 19.11, Problem 19.19Q

Interpretation Introduction

Interpretation:

The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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 5

Chapter 19.11, Problem 19.19Q

Interpretation Introduction

Interpretation:

The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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 6

Chapter 19.11, Problem 19.19Q

Interpretation Introduction

Interpretation:

The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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 19.19Q

Interpretation Introduction

Interpretation:

The structural formula of the peptide val-phe-ala-gly-leu and bond of val-phe-ala-gly-leu that would be cleaved by chymotrypsin and elastase 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

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Answer 11

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

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