Organic Chemistry (9th Edition)
Organic Chemistry (9th Edition)
9th Edition
ISBN: 9780321971371
Author: Leroy G. Wade, Jan W. Simek
Publisher: PEARSON
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Chapter 24.9C, Problem 24.21P

(a)

Interpretation Introduction

To determine: The mechanism for the reaction of the N terminus of the peptide with 2,4-dinitrofluorobenzene.

Interpretation: The mechanism for the reaction of the N terminus of the peptide with 2,4-dinitrofluorobenzene is to be determined.

Concept introduction: The process in which a proper series of amino acids is maintained in the  peptide chain is known as edmann degradation. this process includes the labelling of terminal amino residue  followed by the cleavage of this terminal amino residue from the peptide chain. the peptide bonds between other amino acids do not get disturb during this process.

(b)

Interpretation Introduction

To determine: The reason that the Edman degradation is usually preferred over the Sanger method.

Interpretation: The reason that the Edman degradation is usually preferred over the Sanger method is to be determined.

Concept introduction: The process in which a proper series of amino acids is maintained in the  peptide chain is known as edmann degradation. this process includes the labelling of terminal amino residue  followed by the cleavage of this terminal amino residue from the peptide chain. the peptide bonds between other amino acids do not get disturb during this process.

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Determine the primary structure of an octapeptide from the following data: Acid-catalyzed hydrolysis gives 2 Arg, Leu, Lys, Met, Phe, Ser, and Tyr. Carboxypeptidase A releases Ser. Edman’s reagent releases Leu. Treatment with cyanogen bromide forms two peptides with the following amino acid compositions: 1. Arg, Phe, Ser 2. Arg, Leu, Lys, Met, Tyr Trypsin-catalyzed hydrolysis forms the following two amino acids and two peptides: 1. Arg 2. Ser 3. Arg, Met, Phe 4. Leu, Lys, Tyr
A peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide produces fragments with the following sequences: Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe   What information do this result give about the sequence of the peptide? Explain how you arrived on your answer. a) The sequence is: Met-Val-Glu-Phe-Glu-Gly-Lys-Phe-Met-Ser-Leu-Arg b) The sequence is: Met-Ser-Leu-Arg-Met-Val-Glu-Phe-Glu-Gly-Lys-Phe c) The sequence is: Met-Val-Glu-Phe-Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe d) The sequence is: Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe-Met Val-Glu-Phe
Ph (c) For the peptide coupling reaction shown below, answer the following questions: H₂N. BOP = OH + HSO4 H₂N -N Me₂N-P Me₂N NMe2 O PF6 CH3 BOP, Hünig's base Hünig's base = ایک Dipeptide (i) Give reagents and a curved arrow mechanism for the preparation of alanine tert-butyl ester hydrogen sulfate from alanine. (ii) Provide reagents and a curved arrow mechanism for the formation of Cbz protected glutamine from glutamine hydrogen chloride. (iii) Provide a curved arrow mechanism for the peptide coupling detailed in part (c).

Chapter 24 Solutions

Organic Chemistry (9th Edition)

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