EBK ORGANIC CHEMISTRY
8th Edition
ISBN: 8220102744127
Author: Bruice
Publisher: PEARSON
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Textbook Question
Chapter 21, Problem 69P
Reaction 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
2. Gly, His, Ala
3. Glu, Val, Ser
4. Leu, Glu, Ser
5. Met, Ala, Gly
6. Ser, Lys, Val
7. Glu, His
8. Leu, Lys, Trp
9. Lys, Ser
10. Glu, His, Val
11. Trp, Leu, Glu
12. Ala, Met
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Reaction 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, Met
8. The following proteins represent a wide range of molecular weights and
isoelectric points. Mr is the molecular weight of a single protein chain.
• Protein 1: Mr 68,544; pl 6.11 (monomer)
• Protein 2: Mr 29,041; pl 5.32 (dimer)
• Protein 3: Mr 15,805; pl 5.7 (dimer)
• Protein 4: Mr 12,165; pl 4.74
a. Which protein is the most acidic? Explain your answer.
b. Which protein will migrate the slowest in an SDS-PAGE? Explain your
answer.
c. In what order will these proteins elute from a cation exchanger at pH 8?
Explain your answer.
d. In what order will these proteins salt out from a pH 7 solution by the
dropwise addition of saturated ammonium sulfate? Explain your answer.
5
83°F Cloudy
39. Which of the following amino acids has a sulfur-containing side chain?
a. serine
b. cysteine
c. lysine
d. methionine
e. both b and d
40. Which of the following reagents can be used to cleave a tert-butoxycarbonyl (Boc) protecting group from a
peptide?
a. H₂/Pd
b. CF3CO₂H
c. Na2CO3, H₂O
d. LiAlH4
Chapter 21 Solutions
EBK ORGANIC CHEMISTRY
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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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.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_forwardOn 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_forwardHow many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?arrow_forward
- A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forwardWhat special role does the amino acid cysteine have in the peptides vasopressin and oxytocin?arrow_forward
- Glutathione (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_forward22-61 Polyglutamic acid (a polypeptide chain made only of glutamic acid residues) has an a-helix conformation below pH 6.0 and a random-coil conformation above pH 6.0. What is the reason for this conformational change?arrow_forwardDrawing Peptide Structures Draw the tripeptide that would result from cysteine attaching to the previous dipeptide on the acidic side.arrow_forward
- 22-71 Which amino acid side chain is most frequently involved in denaturation by reduction?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_forwardVasopressin is a peptide hormone synthesized by the hypothalamus; in its reduced form it has the structure shown. NH2 HS H H H H H *H3N° NH2 N' SH NH2 ОН Vasopressin NH *H2N= NH2 This structure is incorrect in that one of the amino acids is shown in the D-configuration, rather than the L-. Which one is it? What is the amino acid sequence of this peptide? Enter your answer using the single letter abbretiavions for the amino acids; i.e. GPT, not Gly-Pro-Thr. What is the net charge of this peptide at physiological pH? ZI IZ ZI IZ ZIarrow_forward
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