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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Done 11:14 ⚫ worksheets.beyondlabz.com 5 (a). Using the peak information you listed in the tables for both structures, assign each peak to that portion of the structure that produces the peak in the NMR spectrum. Draw this diagram on your own sheet of paper and attach the sketch of your drawing to this question. Question 6 5 (b). Using the peak information you listed in the tables for both structures, assign each peak to that portion of the structure that produces the peak in the NMR spectrum. Draw this diagram on your own sheet of paper and attach the sketch of your drawing to this question. Question 7 6. Are there any differences between the spectra you obtained in Beyond Labz and the predicted spectra? If so, what were the differences? <

2. Predict the NMR spectra for each of these two compounds by listing, in the NMR tables below, the chemical shift, the splitting, and the number of hydrogens associated with each predicted peak. Sort the peaks from largest chemical shift to lowest. **Not all slots must be filled** Peak Chemical Shift (d) 5.7 1 Multiplicity multiplate .......... 5.04 double of doublet 2 4.98 double of doublet 3 4.05 doublet of quartet 4 5 LO 3.80 quartet 1.3 doublet 6 Peak Chemical Shift (d) Multiplicity

Interpreting NMR spectra is a skill that often requires some amount of practice, which, in turn, necessitates access to a collection of NMR spectra. Beyond Labz Organic Synthesis and Organic Qualitative Analysis have spectral libraries containing over 700 1H NMR spectra. In this assignment, you will take advantage of this by first predicting the NMR spectra for two closely related compounds and then checking your predictions by looking up the actual spectra in the spectra library. After completing this assignment, you may wish to select other compounds for additional practice. 1. Write the IUPAC names for the following two structures: Question 2 Question 3 2. Predict the NMR spectra for each of these two compounds by listing, in the NMR tables below, the chemical shift, the splitting, and the number of hydrogens associated with each predicted peak. Sort the peaks from largest chemical shift to lowest. **Not all slots must be filled**

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).

Expert Solution & Answer

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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

Expert Solution & Answer

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

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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

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).