Organic Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
8th Edition
ISBN: 9780134473147
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Textbook Question
Chapter 21.13, Problem 39P
A decapeptide undergoes partial hydrolysis to give peptides whose amino acid compositions are shown. Reaction of the intact decapeptide with Edman’s reagent releases PTH-Gly. What is the sequence of the decapeptide?
1. Ala, Trp
2. Val, Pro, Asp
3. Pro,Val
4. Ala,Glu
5. Trp, Ala, Arg
6. Arg, Gly
7. Glu, Ala, Leu
8. Met, Pro, Leu, Glu
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A decapeptide undergoes partial hydrolysis to give peptides whose amino acid compositions are shown. Reaction of the intact decapeptide with Edman’s reagent releases PTH-Gly. What is the sequence of the decapeptide? 1. Ala, Trp 3. Pro, Val 5. Trp, Ala, Arg 7. Glu, Ala, Leu
2. Val, Pro, Asp 4. Ala, Glu 6. Arg, Gly 8. Met, Pro, Leu, Glu
Consider the following peptide : Phe – Glu – Ser – Met and Val – Trp – Cys – Leu. Do these peptides have different net charges at (a) pH 1? (b) pH 7? Indicate the charges at both pH values
Pentapeptide has a sequence of APEDS
Structure of pentapeptide in its proper ionization state at pH 7.0
what is the pI of pentapeptide?
Chapter 21 Solutions
Organic Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
Ch. 21.1 - a. Explain why, when the imidazole ring of...Ch. 21.2 - a. Which isomer(R)-alanine or (S)-alanineis...Ch. 21.2 - Prob. 4PCh. 21.3 - Prob. 5PCh. 21.3 - Prob. 6PCh. 21.3 - Draw the predominant form for glutamate in a...Ch. 21.3 - a. Why is the pKa of the glutamate side chain...Ch. 21.4 - Calculate the pI of each of the following amino...Ch. 21.4 - a. Which amino acid has the lowest pI value? b....Ch. 21.4 - Prob. 12P
Ch. 21.4 - Prob. 13PCh. 21.4 - Explain why the pI of lysine is the average of the...Ch. 21.5 - What aldehyde is formed when valine is treated...Ch. 21.5 - Prob. 16PCh. 21.5 - Prob. 17PCh. 21.5 - Prob. 18PCh. 21.5 - Prob. 19PCh. 21.6 - Why is excess ammonia used in the preceding...Ch. 21.6 - Prob. 21PCh. 21.6 - What amino acid is formed using the...Ch. 21.6 - Prob. 23PCh. 21.6 - What amino acid is formed when the aldehyde used...Ch. 21.7 - Esterase is an enzyme that catalyzes the...Ch. 21.8 - Draw the tetrapeptide Ala-Thr-Asp-Asn and indicate...Ch. 21.8 - Draw the resonance contributors of the peptide...Ch. 21.8 - Which bonds in the backbone of a peptide can...Ch. 21.9 - An opioid pentapeptide has the following...Ch. 21.9 - What is the configuration about each of the...Ch. 21.9 - Glutathione is a tripeptide whose function is to...Ch. 21.10 - What dipeptides would be formed by heating a...Ch. 21.10 - Suppose you are trying to synthesize the dipeptide...Ch. 21.10 - Show the steps in the synthesis of the...Ch. 21.10 - a. Calculate the overall yield of bradykinin when...Ch. 21.11 - Show the steps in the synthesis of the...Ch. 21.13 - Prob. 37PCh. 21.13 - In determining the primary structure of insulin,...Ch. 21.13 - A decapeptide undergoes partial hydrolysis to give...Ch. 21.13 - Explain why cyanogen bromide does not cleave on...Ch. 21.13 - Indicate the peptides produced from cleavage by...Ch. 21.14 - Prob. 43PCh. 21.14 - Three peptides were obtained from a trypsin...Ch. 21.14 - Prob. 45PCh. 21.15 - How would a protein that resides in the nonpolar...Ch. 21.16 - a. Which would have the greatest percentage of...Ch. 21.17 - When apples that have been cut are exposed to...Ch. 21 - Glycine has pK2 values of 2.34 and 9.60. At what...Ch. 21 - Prob. 50PCh. 21 - A titration curve is a plot of the pH of a...Ch. 21 - Prob. 52PCh. 21 - Aspartame (its structure is on page 1007) has a pl...Ch. 21 - Draw the form of aspartate that predominates at...Ch. 21 - Show how phenylalanine can be prepared by...Ch. 21 - A professor was preparing a manuscript for...Ch. 21 - What aldehydes are formed when the following amino...Ch. 21 - Prob. 58PCh. 21 - Determine the amino acid sequence of a polypeptide...Ch. 21 - Prob. 60PCh. 21 - Prob. 61PCh. 21 - Which is the more effective buffer at...Ch. 21 - Identify the location and type of charge on the...Ch. 21 - Draw the product obtained when a lysine side chain...Ch. 21 - After the polypeptide shown below was treated with...Ch. 21 - Treatment of a polypeptide with 2-mercaptoethanol...Ch. 21 - Show how aspartame can be synthesized using DCCD.Ch. 21 - -Amino acids can be prepared by treating an...Ch. 21 - Reaction of a polypeptide with carboxypeptidase A...Ch. 21 - a. How many different octapeptides can be made...Ch. 21 - Glycine has pKa values of 2.3 and 9.6. Do you...Ch. 21 - A mixture of 15 amino acids gave the fingerprint...Ch. 21 - Write the mechanism for the reaction of an amino...Ch. 21 - Prob. 74PCh. 21 - Show how valine can be prepared by a. a...Ch. 21 - The primary structure of -endorphin, a peptide...Ch. 21 - A chemist wanted to test his hypothesis that the...Ch. 21 - Propose a mechanism for the rearrangement of the...Ch. 21 - A normal polypeptide and a mutant of the...Ch. 21 - Determine the amino acid sequence of a polypeptide...
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- Using both three- and one-letter codes for amino acids, write the structures of all possible peptides containing the following amino acids: (a) Val, Ser, Leu (b) Ser, Leu2, Proarrow_forwardA pentapeptide has a sequence of SAPED 1. Draw the pentapeptide in its proper ionization state at pH 7.0 ? 2. What is the pl of the pentapeptide?arrow_forward1. (a) Draw a circle around one amino acidin the structure. ( b) Draw a box around one amino acid side chain. (c) Indicate whether the side chain you chose is hydrophobic or hydrophilic. (d) Draw an arrow pointing to a peptide bond 2. If the peptide segment shown above was part of a beta sheet, which of its functional groups would be involved in forming and stabilizing the beta sheet? 3. Which amino acid (also called amino acid residue)would be more likely to occur on the surface of a protein: an aspartate residue or a methionine residue? Explain your choice.arrow_forward
- Consider a tripeptide (a peptide that's only 3 amino acids long) composed of one molecule each of lysine, leucine, and the hypothetical amino acid lupine (which doesn't actually exist, so don't try to look it up). Lupine has an ionizable side group with a pKa of 6.3. When this tripeptide is dissolved in an aqueous solution at pH 5.0, the net charge on the molecule is +2. Give the charge on the protonated form of the lupine side group, and the charge on the deprotonated form of the lupine side group.arrow_forwardAt very low pH, alanine is a diprotic acid that can be represented as H3N1-CH(CH3)-COOH. The pKa of the carboxyl group is 2.3, and the pKa of the UNH1 3 group is 9.7.(a) At pH 7, what fraction of the amino acid molecules dissolved in an aqueous solution will have the form H3N1-CH(CH3)-COO2?(b) What fraction of the molecules at this pH will havethe form H2N-CH(CH3)-COOH?arrow_forwardConsider the peptide EAHIVR. Write out the sequence of the peptide from N to C in three letter code. Draw the complete structure of the peptide including all peptide bonds and side chains at pH 8.0. Calculate the pI of this peptide. Calculate the net charge of this peptide at pH 2, pH 7, and pH 11. *please show math for # 3 and #4 pls*arrow_forward
- His-Met-Asp-Tyr-Phe-Ser within this peptide, which amino acid residue is the most hydrophobic and why?arrow_forwardThe pKa for the side chain amino group in lysine is 10.4. If we were working at physiological pH 7.4, what would be the ratio of the protonated to unprotonated versions of lysine? a. 1000:1 b. 3:1 c. 1:1000 d. 1:3arrow_forwardA peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 11 and estimate the isoelectric point (pI)(pI) for this peptide.arrow_forward
- Determine the amino acid sequence of a polypeptide from the following data:Complete hydrolysis of the peptide yields Ala, Arg, Gly, 2 Lys, Met, Phe, Pro, 2 Ser, Tyr, and Val.Treatment with Edman’s reagent releases PTH-Val.Carboxypeptidase A releases Ala. Treatment with trypsin yields the following three peptides:1. Gly, Lys, Met, Tyr 2. Ala, Lys, Phe, Pro, Ser 3. Arg, Ser, Valarrow_forward. True/ False A. Amino acids found in the living systems are generally in the D-form B. The R-group attached to alfa carbon atom of amino acids are unique for each amino acids. C. Of the 20 essential amino acids, glycine is the only amino acid which is achiral. D. Ions of heavy metals Hg2+ or Pb2+ denature proteins by combining with the amino groups. E. Denaturation of protein involves the breakdown of secondary, tertiary and quaternary structure. F. Cysteine is the only amino acid that can form a disulfide bridge. G. Both the poly saccharides and proteins are polymers. H. Hydrogen bonding is responsible for the secondary structure of Proteins. I. When proteins are hydrolyzed, smaller peptides and amino acids are produced. J. When simple lipids are hydrolyzed glycerol an alcohol as well as fatty acids and their salts are produced.arrow_forwardWrite out the steps for the synthesis of each peptide using the Merrifieldmethod: Phe–Gly–Ala–Ilearrow_forward
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