Organic Chemistry - Standalone book
10th Edition
ISBN: 9780073511214
Author: Francis A Carey Dr., Robert M. Giuliano
Publisher: McGraw-Hill Education
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Chapter 26, Problem 42P
Interpretation Introduction
Interpretation:
The protected amino acid that should be anchored to the solid support in the first step of a synthesis of oxytocin by the Merrifield method is to be determined.
Concept Introduction:
Merrifield method of peptide synthesis is carried out on a solid
The synthesis starts with anchoring the C terminus of the peptide chain to the polymer via nucleophilic substitution of chlorine in the
The peptide chain is assembled by successive reaction between the amino group of the anchored amino acid/chain with the carboxyl group of the next
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What would be the overall yield of a peptide containing 15 amino acids if the yield for the incorporation of each is 80%?
Amino 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.
Another method to form a peptide bond involves a two-step process
Conversion of a Boc-protected amino acid to a p-nitrophenyl ester.
Why does a p-nitrophenyl ester “activate” the carboxy group of thefirst amino acid to amide formation?
Chapter 26 Solutions
Organic Chemistry - Standalone book
Ch. 26.1 - Prob. 1PCh. 26.2 - Prob. 2PCh. 26.2 - Prob. 3PCh. 26.3 - Prob. 4PCh. 26.3 - Prob. 5PCh. 26.4 - Prob. 6PCh. 26.4 - Prob. 7PCh. 26.4 - Prob. 8PCh. 26.5 - Prob. 9PCh. 26.6 - Prob. 10P
Ch. 26.6 - Prob. 11PCh. 26.6 - Prob. 12PCh. 26.7 - Prob. 13PCh. 26.7 - Prob. 14PCh. 26.7 - Prob. 15PCh. 26.7 - Prob. 16PCh. 26.7 - Prob. 17PCh. 26.9 - Prob. 18PCh. 26.10 - Digestion of the tetrapeptide of Problem 26.18...Ch. 26.12 - Prob. 20PCh. 26.12 - Prob. 21PCh. 26.15 - Prob. 22PCh. 26.15 - Prob. 23PCh. 26.16 - Prob. 24PCh. 26.17 - Prob. 25PCh. 26.18 - Prob. 26PCh. 26 - Prob. 27PCh. 26 - Prob. 28PCh. 26 - Prob. 29PCh. 26 - Prob. 30PCh. 26 - Prob. 31PCh. 26 - Prob. 32PCh. 26 - Prob. 33PCh. 26 - Prob. 34PCh. 26 - Prob. 35PCh. 26 - Prob. 36PCh. 26 - Prob. 37PCh. 26 - Prob. 38PCh. 26 - Prob. 39PCh. 26 - Prob. 40PCh. 26 - If you synthesized the tripeptide Leu-Phe-Ser from...Ch. 26 - Prob. 42PCh. 26 - Prob. 43PCh. 26 - Prob. 44PCh. 26 - Prob. 45DSPCh. 26 - Prob. 46DSPCh. 26 - Prob. 47DSPCh. 26 - Prob. 48DSPCh. 26 - Prob. 49DSPCh. 26 - Prob. 50DSP
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- Another method to form a peptide bond involves a two-step process:[1] Conversion of a Boc-protected amino acid to a p-nitrophenyl ester.[2] Reaction of the p-nitrophenyl ester with an amino acid ester.a. Why does a p-nitrophenyl ester “activate” the carboxy group of the first amino acid to amide formation? b. Would a p-methoxyphenyl ester perform the same function? Why or why not?arrow_forward14. Identify one amino acid from each of the following categories: H2N CH- C-OH H,N CH-O HO- H,N -CH- C-OH I CH, II II CH, CH-OH C=O CH3 CH3 OH H2N -CH- OH H2N-CH- C OH CH2 H2N CH-C-OH CH2 CH2 CH2 CH2 CH3 CH3 IV VIarrow_forward13. Explain why the dansyl chloride treatment of a single polypeptide chain followed by its complete acid hydrolysis yields several dansylated amino acids.arrow_forward
- For lysine and arginine, the isoelectric point, pI, occurs at a pH where the net charge on the nitrogen-containing groups is +1 and balances the charge of -1 on the a-carboxyl group. Calculate pI for these amino acids.arrow_forwardGlycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that the pKa¹ and pKa² of glycine are 2.34 and 9.60, respectively. Calculate the concentration of the dissociated amino acid in terms of the undissociated amino acid, if [x] and [y] are the concentrations of dissociated and undissociated amino acid, respectively.arrow_forwardExplain why the pI of lysine is the average of the pKa values of its two protonated amino groups.arrow_forward
- which of the amino acid will elute first in a cation-exchange column using a buffer at pH 7? Gly or Valarrow_forwardThree peptides were obtained from a trypsin digestion of two different polypeptides. In each case, indicate the possible sequences from the given data and tell what further experiment should be carried out in order to determine the primary structure of the polypeptide. a. polypeptide I: 1. Val-Gly-Asp-Lys 2. Leu-Glu-Pro-Ala-Arg 3. Ala-Leu-Gly-Asp b. polypeptide II: 1. Val-Leu-Gly-Glu 2. Ala-Glu-Pro-Arg 3. Ala-Met-Gly-Lysarrow_forwardDraw the structure of the peptide ENDQCW. Draw the stereochemistry of the amino acids. Show the ionization state that would be the major form at pH 1. What is the isoelectric point of the peptide?arrow_forward
- For aspartic and glutamic acids, the isoelectric point occurs at a pH where the net charge on the two carboxyl groups is -1 and balances the charge of +1 on the a-amino group. Calculate pI for these amino acids.arrow_forwardAnother method to form a peptide bond involves a two-step process Reaction of the p-nitrophenyl ester with an amino acid ester. Why does a p-nitrophenyl ester “activate” the carboxy group of thefirst amino acid to amide formation?arrow_forwardIf you were to design a small peptide with a large net negative charge at physiological pH, which amino acid residues should predominate?arrow_forward
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