Organic Chemistry, 12e Study Guide/Student Solutions Manual
12th Edition
ISBN: 9781119077329
Author: T. W. Graham Solomons, Craig B. Fryhle, Scott A. Snyder
Publisher: WILEY
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Chapter 24, Problem 21P
Interpretation Introduction
Interpretation:
The structural feature of polyglutamic acid and the chemical change for given transformation are to be explained.
Concept introduction:
The
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Serine esterase contains a catalytic triad at its active site. Which amino acid in serine esterase is responsible for mediating general acid catalysis for the breakdown of tetrahedral intermediate to the carboxyl product?
Explain.
The amino acid sequence shown below is a short excerpt (residues 130-172) from the rod domain of an
a-keratin-like protein. Predict the effect of each of the amino acid substitutions (stabilize, destabilize, no effect) and
explain your reasoning.
130 - ATEFKTRFDDAALRANDIQL VIRSNEITADLIKDRLDQITTYY - 172
a) Substitution of S in place of A at position 140.
b) Substitution of V in place of I at position 147.
Outline the steps needed to synthesize the tetrapeptide Ala–Leu–Ile–Gly using the Merrifield technique.
Chapter 24 Solutions
Organic Chemistry, 12e Study Guide/Student Solutions Manual
Ch. 24 - Prob. 1PPCh. 24 - Practice Problem 24.2 The guanidino group NHNHCNH2...Ch. 24 - Prob. 3PPCh. 24 - Prob. 4PPCh. 24 - Prob. 5PPCh. 24 - Prob. 6PPCh. 24 - Prob. 7PPCh. 24 - Practice Problem 24.8
Glutathione is a tripeptide...Ch. 24 - Prob. 9PPCh. 24 - Prob. 10PP
Ch. 24 - Prob. 11PPCh. 24 - Practice Problem 24.12 Show all steps in the...Ch. 24 - Practice Problem 24.13 The synthesis of a...Ch. 24 - Practice Problem 24.14
The terminal carboxyl...Ch. 24 - Prob. 15PPCh. 24 - Prob. 16PPCh. 24 - (a) Which amino acids in Table 24.1 have more than...Ch. 24 - Prob. 18PCh. 24 - 24.19 (a) On the basis of the following sequence...Ch. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - The enzyme lysozyme and its mechanism are...Ch. 24 - Prob. 2LGP
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- Give the sequence of the following tetrapeptide:arrow_forwardTaking the structure of the amino acids into account, give a comparative discussion of these pK values : Alanine : 2.34 : 6.1 : 9.70 Histidine: 1.82 : 9.17arrow_forwardFor the peptide Ala‑Arg‑Lys‑Ala‑Asn‑Ser‑Ala‑Ser, what would be the expected charges at pH 1, 7,pH 1, 7, and 13?arrow_forward
- Suggest a scheme you will follow to synthesise the dipeptide Ala-Glyarrow_forwardDraw the structure of the predominant form of(a) isoleucine at pH 11.arrow_forwardAmino Acids and Proteins 1. What are the structural features of amino acids with an emphasis on essential amino acids? 2. Write the properties of amino acids: zwitterion, pka, pKb, amphoteric character, isoelectric point, and electrophoresis. 3. Write the mechanism of peptide bond formation and what are its structural features. 4. What are the different types of proteins and their function? 5. Explain the meaning and importance of the primary, secondary, tertiary, and quaternary structures of a protein and the factors that cause its denaturation.arrow_forward
- A 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_forwardDraw the structure of the tetrapeptide Asp-Arg-Val-Tyr. Please show the appropriate stereochemistry of the natural amino acids in the resulting peptide. Please draw all ionizable groups in their neutral form.arrow_forwardExplain why the pI of lysine is the average of the pKa values of its two protonated amino groups.arrow_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_forwardAlthough the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.arrow_forwardReaction of the a-carboxyl group of an amino acid or peptide with phenylisothiocyanate allows for the determination of the amino acid residue in the N- terminus of an unknown peptide O True O Falsearrow_forward
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