EBK ORGANIC CHEMISTRY
8th Edition
ISBN: 8220102744127
Author: Bruice
Publisher: PEARSON
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Question
Chapter 21, Problem 52P
Interpretation Introduction
Interpretation:
The amino acid having greatest amount of negative charge at pH 7.4 has to be identified from amino acids leucine and asparagine.
Concept introduction:
The isoelectric point
The value of
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Check out a sample textbook solutionStudents have asked these similar questions
Which has a higher percentage of negative charge at physiological pH (7.4), leucine with pI = 5.98 or asparagine with pI = 5.43?
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
The amino acid histidine has ionizable groups with pK₁ values of 1.8, 6.0, and 9.2, as shown.
COOH
H¸Ñ—CH
CH₂ H
2
CH
pH =
COO™
H¸Ñ—CH
1.8
pk₁
CH₂ H
lonizable -COOH = -COO-
group
CH
COO™
H₂N-CH
6.0
pK₂2
CH₂ H
-HisH -His
N
CH
COO™
H₂N-CH
9.2
pk
CH₂ H
2
—NH — —NH,
CH
A biochemist makes up 95 mL of a 0.13 M solution of histidine at a pH of 5.3. She then adds 60 mL of 0.10 M HCl. What is the
pH of the resulting solution?
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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- 22-35 Why is histidine considered a basic amino acid when the pKa of its side chain is 6.0?arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forward22-47 How many different tetrapeptides can be made (a) if the peptides contain the residues of asparagine, proline, serine, and metbionine and (b) if all 20 amino acids can be used?arrow_forward
- 22-31 A polypeptide chain is made of alternating valine and phenylalanine. Which part of the polypeptide is polar (hydrophilic)?arrow_forward22-9 What is the difference in structure between tyrosine and phenylalanine?arrow_forward22-84 How many different dipeptides can be made (a) using only alanine, tryptophan, glutamic acid, and arginine and (b) using all 20 amino acids?arrow_forward
- 22-48 How many amino acid residues in the A chain of insulin are the same in insulin from humans, cattle (bovine), hogs, and sheep?arrow_forwardFor the tripeptide GlyAlaCys 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_forward22-89 What kind of noncovalent interaction occurs between the following amino acids? (a) Valine and isoleucine (b) Glutamic acid and lysine (c) Tyrosine and threonine (d) Alanine and alaninearrow_forward
- 22-20 Show how alanine, in solution at its isoelectric point, acts as a buffer (write equations to show why the pH does not change much if we add an acid or a base).arrow_forward22-46 How many different tripeptides can be made (a) using one, two, or three residues each of leucine, threonine, and valine and (b) using all 20 amino acids?arrow_forward22-64 If both cysteine residues on the B chain of insulin were changed to alanine residues, how would it affect the quaternary structure of insulin?arrow_forward
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