CHEM 262 ORG CHEM EBOOK DIGITAL DELIVERY
8th Edition
ISBN: 2818440043505
Author: Bruice
Publisher: PEARSON
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Textbook Question
Chapter 21.6, Problem 24P
What amino acid is formed when the
a. acetaldehyde?
b. 2-methylbutanal?
c. 3- methylbutanal?
Expert Solution & Answer
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Check out a sample textbook solutionStudents have asked these similar questions
Which amino acids on proteins can form glycosidic linkages?
Select one:
a. Cysteine and methionine
b. Tryptophan and phenylalanine
c. Glycine and proline
d. Serine and asparagine
e. Alanine and leucine
Identify the reaction type.
a. hydrolysis (in acid)
b. hydration
c. dehydration
d. acid base
e. esterification
f. amide synthesis
g. hydrolysis (in base)
8. Hydrolysis of the peptide bonds in peptide below would result in
Пн
НзN-CHC-N-CHC-N-CНС-о
CH2
Он
СНCH3
ČH3
CH3
a.
no reaction.
b. a single amino acid.
c. two amino acids.
d. three amino acids.
e. four amino acids.
Chapter 21 Solutions
CHEM 262 ORG CHEM EBOOK DIGITAL DELIVERY
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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- 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_forward4. What is the strongest type of non-covalent interactions that could form between the following amino acids' side chains? a. Valine and Alanine b. Glutamic acid and Serine c. Asparagine and Threonine d. Lysine and Aspartic acidarrow_forwardDisulfide linkages: A. are covalent bonds. B. are a type of electrostatic interaction. C. occur between methionine residues. D. can be disrupted by SDS. E. can only occur within the same polypeptide chain.arrow_forward
- What amino acid is formed when the aldehyde used in the Strecker synthesis is a. acetaldehyde? b. 2-methylbutanal? c. 3-methylbutanal?arrow_forward10. Consider the amino acids glycine, valine 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 valine at its N-terminal amino acid and glycine as its C-terminal amino acid. Circle each peptide bond.arrow_forward7. Draw the structure for each of the following amino acids. For each acid, circle any chiral carbons. a. Lysine b. Aspartate c. Tryptophan d. Alaninearrow_forward
- 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. LiAlH4arrow_forwardalpha-Amino acids can be prepared by treating an aldehyde with ammonia/trace acid, followed by hydrogen cyanide, followed by acid-catalyzed hydrolysis. a. Draw the structures of the two intermediates formed in this reaction. b. What amino acid is formed when the aldehyde that is used is 3-methylbutanal? c. What aldehyde is needed to prepare isoleucine?arrow_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_forward
- Identify the major class of each lipid from its components. a. fatty acids + glycerol b. fatty acids + sphingosine + a carbohydrate c. fatty acids + high-molecular-weight alcohols other than glycerol d. glycerol + fatty acids + phosphate group + choline e. fatty acids + sphingosine + phosphate group + a nitrogen compoundarrow_forward1. What test reagents are used for the alkylation of amino acids (alkylating reagents)? 2. What test reagents are used for acid hydrolyzation of amino acidsarrow_forwardA plat-form molecule of a lipid which is composed of 3 Hydroxyl groups. A. Spingosine B. Fatty acids C. Taurocholine D. Glycerol E. Triglyceridearrow_forward
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