The structural formula of the peptide ala-phe-ala and bond of peptide ala-phe-ala 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 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 19.17Q

(a)

Interpretation Introduction

Interpretation:

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

Concept Introduction:

Refer to part (a).

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Is this aromatic?

CHEM2323 E Tt PS CH03 Draw and name all monobromo derivatives of pentane, C5H11Br. Problem 3-33 Name: Draw structures for the following: (a) 2-Methylheptane (d) 2,4,4-Trimethylheptane Problem 3-35 (b) 4-Ethyl-2,2-dimethylhexane (e) 3,3-Diethyl-2,5-dimethylnonane (c) 4-Ethyl-3,4-dimethyloctane 2 (f) 4-Isopropyl-3-methylheptane KNIE>

Problem 3-42 Consider 2-methylbutane (isopentane). Sighting along the C2-C3 bond: (a) Draw a Newman projection of the most stable conformation. (b) Draw a Newman projection of the least stable conformation. Problem 3-44 Construct a qualitative potential-energy diagram for rotation about the C-C bond of 1,2-dibromoethane. Which conformation would you expect to be most stable? Label the anti and gauche conformations of 1,2- dibromoethane. Problem 3-45 Which conformation of 1,2-dibromoethane (Problem 3-44) would you expect to have the largest dipole moment? The observed dipole moment of 1,2-dibromoethane is µ = 1.0 D. What does this tell you about the actual conformation of the molecule?

Answer 2

Question

Chapter 19.11, Problem 19.17Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the peptide ala-phe-ala and bond of peptide ala-phe-ala 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 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 peptide tyr-ala-tyr and bond of peptide tyr-ala-tyr 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 19.17Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the peptide ala-phe-ala and bond of peptide ala-phe-ala 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 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 peptide tyr-ala-tyr and bond of peptide tyr-ala-tyr 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 19.17Q

(a)

Interpretation Introduction

Interpretation:

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

Concept Introduction:

Refer to part (a).

Expert Solution & Answer

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Answer 5

Chapter 19.11, Problem 19.17Q

(a)

Interpretation Introduction

Interpretation:

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

Concept Introduction:

Refer to part (a).

Answer 6

Chapter 19.11, Problem 19.17Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the peptide ala-phe-ala and bond of peptide ala-phe-ala 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 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 19.17Q

(a)

Interpretation Introduction

Interpretation:

The structural formula of the peptide ala-phe-ala and bond of peptide ala-phe-ala 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 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 peptide tyr-ala-tyr and bond of peptide tyr-ala-tyr 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 peptide tyr-ala-tyr and bond of peptide tyr-ala-tyr 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 peptide tyr-ala-tyr and bond of peptide tyr-ala-tyr 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

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Interpretation: The structural formula of the peptide tyr-ala-tyr and bond of peptide tyr-ala-tyr 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 peptide tyr-ala-tyr and bond of peptide tyr-ala-tyr that would be cleaved by chymotrypsin has to be determined.

Concept Introduction:

Refer to part (a).