Organic Chemistry
4th Edition
ISBN: 9780073402772
Author: Janice G. Smith
Publisher: MCG
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Question
Chapter 29, Problem 29.21P
Interpretation Introduction
Interpretation: The sequence of heptapeptide that contains amino acids Ala, Arg, Glu, Gly, Leu, Phe and Ser from the given experimental data is to be predicted.
Concept introduction: The chemical compounds in which carbon atom is bonded to
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Deduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu,
Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from the
heptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptide
with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide
with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and the
tripeptides Gly-Ala-Ser and Ala-Ser-Arg.
Deduce the sequence of a pentapeptide that contains the amino acids Ala, Glu, Gly, Ser, and Tyr, from the following experimental data. Edman degradation cleaves Gly from the pentapeptide, and carboxypeptidase forms Ala and a tetrapeptide. Treatment of the pentapeptide with chymotrypsin forms a dipeptide and a tripeptide. Partial hydrolysis forms Gly, Ser, and the tripeptide Tyr–Glu–Ala.
An octapeptide contains the following amino acids: Arg, Glu, His, Ile, Leu, Phe, Tyr, and Val. Carboxypeptidase treatment of the octapeptide forms Phe and a heptapeptide. Treatment of the octapeptide with chymotrypsin forms two tetrapeptides, A and B. Treatment of A with trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Glu (octapeptide), Glu (A), Ile (B), Glu (C), and Val (D). Partial hydrolysis of tetrapeptide B forms Ile–Leu in addition to other products. Deduce the structure of the octapeptide and fragments A–D.
Chapter 29 Solutions
Organic Chemistry
Ch. 29 - Prob. 29.1PCh. 29 - Problem 29.2
What form exists at the isoelectric...Ch. 29 - Problem 29.3
Explain why the of the group of an...Ch. 29 - Problem 29.5
What -halo carbonyl compound is...Ch. 29 - Problem 29.6
The enolate derived from diethyl...Ch. 29 - Problem 29.7
What amino acid is formed when is...Ch. 29 - Problem 29.8
What aldehyde is needed to synthesize...Ch. 29 - Prob. 29.8PCh. 29 - Prob. 29.9PCh. 29 - Prob. 29.10P
Ch. 29 - Prob. 29.11PCh. 29 - Problem 29.13
What alkene is needed to synthesize...Ch. 29 - Problem 29.14
Draw the structure of each peptide....Ch. 29 - Name each peptide using both the one-letter and...Ch. 29 - Prob. 29.15PCh. 29 - Prob. 29.16PCh. 29 - Problem 29.18
Glutathione, a powerful antioxidant...Ch. 29 - Problem 29.19
Draw the structure of the...Ch. 29 - Problem 29.20
Give the amino acid sequence of an...Ch. 29 - a What products are formed when each peptide is...Ch. 29 - Prob. 29.21PCh. 29 - Devise a synthesis of each peptide from amino acid...Ch. 29 - Devise a synthesis of the following dipeptide from...Ch. 29 - Prob. 29.24PCh. 29 - Consider two molecules of a tetrapeptide composed...Ch. 29 - What types of stabilizing interactions exist...Ch. 29 - Prob. 29.27PCh. 29 - Draw the product formed when the following amino...Ch. 29 - With reference to the following peptide: a...Ch. 29 - Devise a synthesis of the following dipeptide from...Ch. 29 - Prob. 29.31PCh. 29 - Prob. 29.32PCh. 29 - Histidine is classified as a basic amino acid...Ch. 29 - Tryptophan is not classified as a basic amino acid...Ch. 29 - What is the structure of each amino acid at its...Ch. 29 - To calculate the isoelectric point of amino acids...Ch. 29 - What is the predominant form of each of the...Ch. 29 - 29.37 What is the predominant form of each of the...Ch. 29 - a. Draw the structure of the tripeptide A–A–A, and...Ch. 29 - Draw the organic product formed when the amino...Ch. 29 - 29.39 Draw the organic products formed in each...Ch. 29 - 29.40 What alkyl halide is needed to synthesize...Ch. 29 - 29.41 Devise a synthesis of threonine from diethyl...Ch. 29 - 29.42 Devise a synthesis of each amino acid from...Ch. 29 - Prob. 29.45PCh. 29 - Prob. 29.46PCh. 29 - Prob. 29.47PCh. 29 - Prob. 29.48PCh. 29 - Prob. 29.49PCh. 29 - 29.48 Brucine is a poisonous alkaloid obtained...Ch. 29 - Prob. 29.51PCh. 29 - Prob. 29.52PCh. 29 - Draw the structure for each peptide: (a) Phe–Ala;...Ch. 29 - 29.52 For the tetrapeptide Asp–Arg–Val–Tyr:
a....Ch. 29 - Prob. 29.55PCh. 29 - Explain why a peptide CN bond is stronger than an...Ch. 29 - Prob. 29.57PCh. 29 - 29.55 Draw the amino acids and peptide fragments...Ch. 29 - Prob. 29.59PCh. 29 - Prob. 29.60PCh. 29 - Prob. 29.61PCh. 29 - 29.59 An octapeptide contains the following amino...Ch. 29 - Prob. 29.63PCh. 29 - Prob. 29.64PCh. 29 - Draw all the steps in the synthesis of each...Ch. 29 - 29.62 Write out the steps for the synthesis of...Ch. 29 - 29.64 Another method to form a peptide bond...Ch. 29 - Prob. 29.68PCh. 29 - Prob. 29.69PCh. 29 - Which of the following amino acids are typically...Ch. 29 - After the peptide chain of collagen has been...Ch. 29 - Prob. 29.72PCh. 29 - Prob. 29.73PCh. 29 - 29.70 The anti-obesity drug orlistat works by...Ch. 29 - Prob. 29.75P
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Similar questions
- For the tripeptide SerValMet a. What amino acid is located at the peptides N-terminal end? b. What amino acid is located at the peptides C-terminal end? c. How many peptide bonds are present? d. How many amide linkages are present?arrow_forwardGlutathione (G-SH), one of the most common tripeptides in animals, plants, and bacteria, is a scavenger of oxidizing agents. In reacting with oxidizing agents, glutathione is converted to G-S-S-G. (a) Name the amino acids in this tripeptide. (b) What is unusual about the peptide bond formed by the N-terminal amino acid? (c) Write a balanced half-reaction for the reaction of two molecules of glutathione to form a disulfide bond. Is glutathione a biological oxidizing agent or a biological reducing agent? (d) Write a balanced equation for reaction of glutathione with molecular oxygen, O2 to form G-S-S-G and H2O. Is molecular oxygen oxidized or reduced in this process?arrow_forwardFor the tripeptide GlyAlaCys a. What amino acid is located at the peptides N-terminal end? b. What amino acid is located at the peptides C-terminal end? c. How many peptide bonds are present? d. How many amide linkages are present?arrow_forward
- On complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments: Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids?arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forwardReaction of a polypeptide with carboxypeptidase A releases Met. The polypeptide undergoes partial hydrolysis to give the following peptides. What is the sequence of the polypeptide? 1. Ser, Lys, Trp 4. Leu, Glu, Ser 7. Glu, His 10. Glu, His, Val 2. Gly, His, Ala 5. Met, Ala, Gly 8. Leu, Lys, Trp 11. Trp, Leu, Glu 3. Glu, Val, Ser 6. Ser, Lys, Val 9. Lys, Ser 12. Ala, Metarrow_forward
- A tripeptide on hydrolysis produced glycine, alanine and leucine. The structures of these amino acids are shown below. On reaction with Edman’s reagent, leucine was released as the phenylhydantoin. Treatment of the tripeptide with carboxypeptidase gave glycine. Draw the structure of the tripeptide.arrow_forwardA normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutant poly peptide differ by one amino acid. The fingerprints of the peptides obtained from the two polypeptides are shown below. What kind of amino acid substitution occurred as a result of the mutation? (That is, is the substituted amino acid more or less polar than the original amino acid? Is its pI lower or higher?)arrow_forwardThe compound shown below is used to fluorescently label proteins: но. HO Which of the following statements about the reactivity of compound (1) with proteins is CORRECT? Compound (1) reacts with tyrosine residues in the protein to form a stable thiourea linkage. O Compound (I) reacts with tyrosine residues in the protein to form a stable amide linkage. O Compound (1) reacts with lysine residues in the protein to form a stable amide linkage. O Compound (I) reacts with lysine residues in the protein to form a stable thiourea linkage.arrow_forward
- There is a hexapeptide, and its primary structure is written down according to the following experimental results, and the analysis process is briefly written down: (1) DNP-Ala was obtained by DNFB reaction; (2) DNP-Ile was obtained by reaction with DNFB after hydrazine hydrolysis; (3) Two tripeptides were obtained by reaction with cyanogen bromide, then DNP-Leu and DNP-Ala were obtained by reaction with DNFB; (4) Fragments containing 1, 2 and 3 amino acids were obtained by trypsin hydrolysis, and the Sakakuchi reaction of the last two fragments was positive.arrow_forward2arrow_forwardA tripeptide undergoes complete hydrolysis and the resulting mixture contains only phenylalanine and glycine. Draw all possible sequences for the original tripeptide.arrow_forward
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