Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Textbook Question
Chapter 21.4, Problem 10P
Calculate the pI of each of the following amino acids:
a. asparagine
b. arginine
c. serine
d. aspartate
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26. Almost all proteins are composed from a set of about
amino acids.
20
d. 50
a. 4
27.
a. 5
b. 10
amino acids are considered essential.
b. 10
C.
C.
15
d. 20
refer to the structure
1. This drug may likely bind to what protein?
a. Alphaglycoprotein
b. Bilirubin
c. Albumin
d. Globulin
2. What is the IUPAC name of this compound?
a. Octanoic acid
b. 2 – propylpentanoic acid
c. 1 – butylbutanoic acid
d. 2 – methylheptanoic acid
3. This drug may likely affects what neurotransmitter?
a. Norepinephrine
b. Gamma amino butyric acid
c. Glutamate
d. Dopamine
4. This drug affects what type of ion gated channel?
a. Sodium
b. Potassium
c. Calcium
d. Both A and B
e. Both A and C
f. Both B and C
5. This drug is a powerful
a. Antiparkinsonism
b. Anticonvulsant
c. Antipsychotic
d. Antidepressant
34. Which of the following is not a property of amino acids
a. Buffer
35. The protein primary structure is held together by
a. Hydrogen bonds
b. Isoelectric point
C.
Zwitterions
d. Insoluble in water
b. Disulfide bonds
c. Peptide bonds
d. Protein bonds
Chapter 21 Solutions
Organic Chemistry (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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- of a protein. 15. The amino acid sequence is the a. primary structure b. secondary structure c. tertiary structure d. quaternary structure e. both secondary and tertiaryarrow_forward1. The pyrimidine heterocyclic system is present in the structure of drugs: A. Theophylline B. Folic acid C. Phenazepam D. Aminazinarrow_forwardDraw each amino acid in its dipolar ion form. a. Val b. Phe c. Tyr d. Cysarrow_forward
- Which of the following is not used to classify amino acid side chains? a. non-polar b. neutral c. acidic d. basic e. polararrow_forwardNonearrow_forwarda. Tyrosine b. Alanine c. Leucine d. Asparagine 5. Draw a picture showing the details of the hydrogen bonding between the side chain and the protein backbone for any amino acid residues from exercise 4 that are capable.arrow_forward
- what explains the pH dependence of prior protein folding? a. Hydrogen ions interfere with disulfide bond formation. b. Hydrogen ions interfere with hydrogen bonding to form secondary c. Hydrogen ions interfere with hydrophobic interactions in the proteins d. Hydrogen ions interfere with the primary amino acid sequence what is the osmolarity when 1.5 mole MgC12 is added to 1 liter of water? a. 1.2 Osmol 3 Osmol c. 4.5 Osmol d. 6 Osmol What is the pH of 1.75M benzoic acid given Ka-6.4-10^-5 a. 1.35 b. 1.98. c. 4.20 d. 4.96 What type of bonds are sodium and fluorine likely to form given electronegativity values of .93 and 3.98 for sodium and fluorine, respectively? a. Covalent b. Hydrogen c. Ionic d. Metallic How many electrons are present within the valence shell of an atom that satisfies the octet rule? a. b. 2 C. d. 8 What concentration of acid is used to create a 10mM pH 7.6 sodium phosphate buffer with a pKa of 7.2? a. .003M b. .007M C. 1.2M d. 2.85M What is the sum of pH and pOH…arrow_forward9) A COOH H₂N-C-H CH₂ CH₂ CH₂ CH₂ NH₂ 2.18 Coo H₂N-C-H CH₂ CH₂ CH₂ 8.95 Coo HN-C-H CH₂ CH₂ CH₂ 1 CH₂ NH₂ 16.53 What is this amino acid and the pl? a) This is arginine and the pl is 8.50 b) This is glutamine and the pl is 5.57 c) This is arginine and the pl is 9.62 Coo H₂N-C-H CH₂ 1 CH₂ CH₂ CH₂ NH₂arrow_forwardi 3. Identify which of the following pairs of amino acid residues can have London dispersion forces between their side chains. a. Alanine and Glycine b. Leucine and Isoleucine Valine and Asparagine C. d. Threonine and Tyrosinearrow_forward
- 4. How is the following amino acid classified? H3Ñ-CHC-o CH2 a. nonpolar b. polar neutral c. polar acidic d. polar basicarrow_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_forwardIn the tetrapeptide Phe-Gln-Trp-His, the C-terminal amino acid is A. Phe B. Trp C. His D. Glnarrow_forward
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