EBK ORGANIC CHEMISTRY
8th Edition
ISBN: 8220102744127
Author: Bruice
Publisher: PEARSON
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Textbook Question
Chapter 21.1, Problem 1P
- a. Explain why, when the imidazole ring of histidine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton.
- b. Explain why. when the guanidino group of arginine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton.
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Explain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton.
A. Draw the structure of L-valine in a strongly basic solution.
B. What is the charge of this amino acid in a strongly basic solution?
C. What is the pH of D at its isoelectric point?
D. Show the structure of this amino acid at its isoelectric point.
E. What is the charge of this amino acid in a strongly acidic solution?
10. Which side chain would most likely be found in the interior of a protein, away
from the aqueous environment?
a.
-CH2OH
b. -CH2SH
с. -СH-CООН
d. -CH2CONH2
e.
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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- 22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forwardArginine exists in two high-pH forms instead of the usual one. Explain why.arrow_forwardFor 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_forward
- D. Consider the amino acids glycine, proline and lysine. a. How many tripeptides can be formed from these three amino acids if each is used only once in the structure? b. Using three-letter abbreviations for the amino acids, give the sequence of each of the possible tripeptides. c. Draw the structure of the dipeptide that has proline at its N-terminal amino acid and glycine as its C-terminal amino acid. Circle each peptide bond.arrow_forwardLysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the α carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.arrow_forward10. Which side chain would most likely be found in the interior of a protein, away from the aqueous environment? a. -CH2OH b. c. -CH2COOH d. -CH2CONH2 |I -CH2SH e.arrow_forward
- Draw the structure of each peptide. Label the N-terminal and C-terminal amino acids and all amide bonds. a. Val–Glu b. Gly–His–Leu c. M–A–T–Tarrow_forwardNot too sure if it's sodium dodecyl sulfate or imidazole.arrow_forwardDraw the structure of each peptide. Label the N-terminal and C-terminal amino acids and all amide bonds. a. Val-Glu b. Gly-His-Leu c. M-A-T-Tarrow_forward
- 1. Determine the isolation points (kasein) of alanine and argininearrow_forward2. Diagram the peptide ACKE at physiological then answer questions a- h. a. Circle one peptide bond. b. Box one alpha carbon in this peptide c. How many peptide bonds are present in this peptide? d. Which amino acid is at the C-terminus? e. Which amino acid is at the N-terminus? f. Label one omega, one phi and one psi bond angle. g. Sketch in one peptide plane. h. Calculate the charge of the peptide at pH 13.arrow_forward1. At what pH is the side chain of arginine 65% ionized? 2. At what pH is glutamate 25% ionized? 3. At what pH is the side chain of histidine 4/5 ionized? 4. At what pH is the side chain of cysteine 15% ionized? 5. At what pH is tyrosine 5/8 ionized?arrow_forward
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