Chapter 19

General, Organic & Biological Chemistry, 5e (Timberlake)
Chapter 19 Amino Acids and Proteins
19.1 Multiple-Choice Questions
1) Which of the following is NOT a function of proteins?

A) provide structural components
B) stores the genetic information of a living organism
C) movement of muscles
D) catalyze reactions in the cells
E) transport substances through the bloodstream
Answer: B
Objective: 19.1
Global Outcomes: GO2
2) Collagen, a protein found in tendons and cartilage, would be classified as a ________ protein.
A) catalytic
B) structural
C) transport
D) storage
E) hormone
Answer: B
Objective: 19.1
3) Wool is primarily made up of

A) protein.
B) carbohydrate.
C) globin.
D) triacylglycerols.
E) enkephalin.
Answer: A
Objective: 19.1
4) Sucrase, the protein that facilitates the hydrolysis of sucrose, would be classified as a ________ protein.
A) transport
B) hormonal
C) catalytic
D) structural
E) contractile
Answer: C
Objective: 19.1
1
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5) The structural formulas of amino acids are the same EXCEPT for the
A) carboxyl group.
B) alpha carbon.
C) amino group.
D) side (R) group.
E) hydrogen bonding.
Answer: D
Objective: 19.1
6) The following amino acid R group chain is
- C HCH3
|
CH3
A) polar.
B) hydrophobic.
C) hydrophilic.
D) acidic.
E) basic.
Answer: B
Objective: 19.1
7) Which of the following would be most likely to be deficient in at least one essential amino acid?
A) eggs
B) milk
C) beans
D) steak
E) ham
Answer: C
Objective: 19.1
8) Amino acids that are not synthesized in the body and must be obtained from the diet are called
A) essential.
B) polar.
C) nonpolar.
D) complete.
E) incomplete.
Answer: A
Objective: 19.1
2
9) Methionine is an amino acid that contains
A) a sulfur atom.
B) a chlorine atom.
C) a sodium atom.
D) a phenyl ring.
E) a heterocyclic ring.
Answer: A
Objective: 19.1
10) A completely vegetarian diet will contain all the essential amino acids if it includes
A) wheat and rice.
B) rice and beans.
C) almonds and walnuts.
D) corn and beans.
E) wheat and corn.
Answer: B
Objective: 19.1
11) Glycine is the only naturally occurring amino acid that is

A) negatively charged.
B) positively charged.
C) neutral.
D) in the L- form.
E) achiral.
Answer: E
Objective: 19.1
12) The side chain for histidine is classified as a ________ R group.

A) basic
B) neutral
C) acidic
D) nonpolar
E) polar
Answer: A
Objective: 19.1
13) A basic amino acid has an R group that contains

A) an amine group.
B) a carboxyl group.
C) a methyl group.
D) an alcohol group.
E) a thiol group.
Answer: A
Objective: 19.1
3
14) At a pH > 9, the zwitterion of glycine (pI=6.0) will have
A) a net positive charge.
B) a net negative charge.
C) an overall charge of zero.
D) low solubility in water.
E) a negative charge on the nitrogen.
Answer: B
Objective: 19.2
15) At a pH < 5, the zwitterion for alanine (pI = 6) will have

A) a net positive charge.
B) a net negative charge.
C) an overall charge of zero.
D) low solubility in water.
E) a negative charge on the carboxyl group.
Answer: A
Objective: 19.2
4
16) What is the structural formula of glutamic acid (pI = 3.2) at pH = 1?
A)
B)
C)
D)
E)
Answer: A
Objective: 19.2
17) Consider a mixture of the amino acids lysine (pI = 9.7), tyrosine (pI = 5.7), and glutamic acid (pI = 3.2)
at a pH 5.7 that is subjected to an electric current. ________ will migrate towards the positive electrode(+).
A) Lysine
B) Tyrosine
C) Glutamic acid
D) All of the amino acids
Answer: C
Objective: 19.2
5
18) Consider a mixture of the amino acids lysine (pI = 9.7), tyrosine (pI = 5.7), and glutamic acid (pI = 3.2)
at a pH 5.7 that is subjected to an electric current. ________ will remain stationary.
A) Lysine
B) Tyrosine
C) Glutamic acid
D) All of the amino acids
Answer: B
Objective: 19.2
19) In a typical amino acid zwitterion, the carboxylate end is

A) positively charged.
B) negatively charged.
C) neutral.
D) soluble in a nonpolar solvent.
E) attached to an amine.
Answer: B
Objective: 19.2
20) The R group for serine is - CH2OH. As a zwitterion, serine has the structural formula
A) CH2OH
|
NH2 C HCOOH
B) CH2OH
|
NH2 C HCOO-
C) CH2O-
+ |
N H3 C HCOOH
D) CH2OH
+ |
N H3 C HCOOH
E) CH2OH
|
H3 C HCOO-
Answer: E
Objective: 19.2
6
21) Which of the following functional groups of an amino acid would be in the ionized state at high pH?
A) O
-COH
B) -CH2OH
C) -CH3
D) O
-CNH2
E)
Answer: A
Objective: 19.2
7
22) Which of the following is the correct structure for Ser-Ala-Asp? The appropriate side chains look like
this.
O
Ala: -CH3; Ser: -CH2OH; Asp: -CH2COH
A) OH COOH
| |
CH3 O CH2 O CH2 O
| | |
H3 N+ C H - C - NH - C H - C - NH - C H - C O-
B) COOH OH
| |
CH2 O CH3 O CH2 O
| | |
C) OH COOH
| |
CH2 O CH2 O CH3 O
| | |
H3 N C H - C - NH - C H - C - NH - C H - C O-
+
D) COOH OH
| |
CH2 O CH2 O CH3 O
| | |
H3 N C H - C - NH - C H - C - NH - C H - C O-
+
E) OH COO-
| |
CH2 O CH3 O CH2 O
| | |
Answer: E
Objective: 19.3
8
23) The peptide bonds that combine amino acids in a protein are
A) ester bonds.
B) ether bonds.
C) amide bonds.
D) glycosidic bonds.
E) sulfide bonds.
Answer: C
Objective: 19.3
24) In the peptide Ala-Try-Gly-Phe, the N-terminal amino acid is

A) alanine.
B) phenylalanine.
C) tryptophan.
D) aspartic acid.
E) glycine.
Answer: A
Objective: 19.3
25) In the peptide Ser-Cys-Ala-Gly, the C-terminal end is

A) serine.
B) serotonin.
C) glycine.
D) glycerine.
E) alanine.
Answer: C
Objective: 19.3
26) Which of the following shows all of the tripeptides that can be formed from one molecule each of
glycine (Gly), valine (Val), and leucine (Leu)?
A) Gly-Val-Leu, Gly-Leu-Val, Val-Leu-Gly, Val-Gly-Leu, Leu-Gly-Val, Leu-Val-Gly
B) Gly-Val-Leu, Gly-Leu-Val, Leu-Gly-Val
C) Val-Gly-Leu, Gly-Val-Leu, Gly-Leu-Val, Leu-Gly-Val
D) Val-Gly-Leu, Gly-Leu-Val
E) Gly-Val-Leu
Answer: A
Objective: 19.3
9
27) Which of the following shows all of the tripeptides that can be formed from one molecule each of
lysine (Lys), threonine (Thr), and histidine (His)?
A) Lys-Thr-His
B) Lys-Thr-His, Lys-His-Thr, His-Thr-Lys, His-Lys-Thr, Thr-Lys-His, Thr-His-Lys
C) Lys-Thr-His, Lys-His-Thr, His-Lys-Thr, Thr-His-Lys
D) Lys-Thr-His, Lys-His-Thr, His-Lys-Thr
E) Lys-Thr-His, Lys-His-Thr
Answer: B
Objective: 19.3
28) A peptide bond contains which kind of functional group?

A) alcohol
B) amine
C) amide
D) carboxylic acid
E) ketone
Answer: C
Objective: 19.3
29) A chain made of more than 50 amino acids is usually referred to as a(n)
A) peptide.
B) protein.
C) enzyme.
D) globulin.
E) hormone.
Answer: B
Objective: 19.4
30) Which of the following is an example of a secondary protein structure?

A) dipeptide
B) triglyceride
C) a helix
D) amino acid
E) fatty acid
Answer: C
Objective: 19.4
10
31) The α helix of the secondary structure of a protein is held together by ________ between two widely
separated parts of a protein chain.
A) hydrogen bonds
B) disulfide bridges
C) salt bridges
D) hydrophilic interactions
E) hydrophobic interactions
Answer: A
Objective: 19.4
32) In the β-pleated sheet secondary structure of a protein, two or more amino acid sequences in separate
parts of the protein are held together
A) in a coil, by hydrogen bonding.
B) in random order, due to hydrophobic interactions.
C) in a triple helix.
D) in a double helix.
E) in a zig-zag conformation, by hydrogen bonding.
Answer: E
Objective: 19.4
33) Enkephalins are polypeptides that have

A) a sweet taste.
B) a bitter taste.
C) extra caloric value.
D) pain-killing properties.
E) hormone activity.
Answer: D
Objective: 19.4
34) Enkephalins, naturally produced opiates in the body, are found in

A) muscles and bone tissue.
B) brain and kidney tissue.
C) thalamus and spinal cord tissue.
D) heart and lung tissue.
E) pancreas and liver tissue.
Answer: C
Objective: 19.4
11
35) The interactions that are important in the secondary structure of a protein are
A) hydrogen bonds.
B) hydrophobic interactions.
C) disulfide bonds.
D) salt bridges.
E) peptide bonds.
Answer: A
Objective: 19.4
36) Which of the following is a secondary protein structure?

A) α helix
B) Ser-Met-Ala-Gly-Ile
C) disulfide bond
D) salt bridges
Answer: A
Objective: 19.4
37) The secondary structure of collagen is distinguished by

A) single α helix strands.
B) double α helix strands.
C) many α helixes wound into fibrils.
D) a braided triple helix.
E) many glycoside links.
Answer: D
Objective: 19.4
38) In insulin, two peptide chains are held together in a single unit by
A) disulfide bridges.
B) hydrogen bonds.
C) salt bridges.
D) a prosthetic group.
E) a β-pleated sheet.
Answer: A
Objective: 19.4
39) Hemoglobin is an example of a protein with

A) primary structure only.
B) two protein chains held together.
C) a globular structure.
D) primarily a β-pleated sheet structure.
E) primarily an α helix structure.
Answer: C
Objective: 19.5
12
40) The heme in hemoglobin is a(n)
A) protein chain.
B) small molecule within a protein.
C) helix area in the hemoglobin molecule.
D) pleated sheet area in the hemoglobin molecule.
E) oxygen molecule within the hemoglobin molecule.
Answer: B
Objective: 19.5
41) Within hemoglobin, the heme functions as

A) a disulfide bridge.
B) an oxygen carrier.
C) a reducing agent.
D) an α subunit.
E) one of the four protein subunits.
Answer: B
Objective: 19.5
42) Hemoglobin has a total of ________ protein chains in its quaternary structure.
A) one
B) two
C) three
D) four
E) five
Answer: D
Objective: 19.5
43) The fibrous protein responsible for the structure of hair and wool is
A) keratin.
B) collagen.
C) endorphin.
D) myosin.
E) casein.
Answer: A
Objective: 19.5
13
44) Which R group would most likely be found in a hydrophobic area of the tertiary structure of a
globular protein?
A) -CH2OH
B) -CH2COO-
C)
D) -CH2CH2CH2CH2 H3
E) O
-CH2 C NH2
Answer: C
Objective: 19.5
45) What type of interaction would you expect between the following R groups in the tertiary structure of
a protein?
-CH2 C O- and -CH2CH2CH2CH2NH3+
A) disulfide bonds
B) salt bridges
C) hydrogen bonds
D) hydrophobic interactions
E) peptide bonds
Answer: B
Objective: 19.5
46) Disulfide bonds in a protein chain connect

A) an amine and a carboxylic acid group.
B) an alcohol and a carboxylic acid group.
C) tryptophan and alanine residues.
D) two cysteine residues.
E) two asparagine residues.
Answer: D
Objective: 19.5
14
47) What kinds of interactions are NOT part of tertiary protein structure?
A) peptide bonds
B) disulfide bonds
C) hydrophilic interactions
D) salt bridges
Answer: A
Objective: 19.5
48) The function of myoglobin is to

A) carry vitamins in the blood.
B) carry oxygen in the blood.
C) support the skeletal muscles.
D) carry oxygen in the muscle.
E) provide strength in cartilage.
Answer: D
Objective: 19.5
49) In sickle-cell anemia, the hemoglobin molecules

A) come apart into separate chains.
B) enlarge to twice normal size.
C) clump together into insoluble fibers.
D) dissolve in the plasma.
E) undergo crenation.
Answer: C
Objective: 19.5
50) Acids and bases denature a protein by disrupting

A) peptide bonds and ionic bonds.
B) amide bonds and alkene bonds.
C) hydrophobic interactions and peptide bonds.
D) ionic bonds and hydrophobic interactions.
E) ionic bonds and hydrogen bonds.
Answer: E
Objective: 19.6
51) Heat denatures a protein by disrupting

A) ionic bonds and peptide bonds.
B) hydrophobic bonds and hydrogen bonds.
C) peptide bonds and hydrophobic bonds.
D) disulfide bonds and peptide bonds.
E) hydrogen bonds and disulfide bonds.
Answer: B
Objective: 19.6
15
52) Denaturation of a protein
A) changes the primary structure of a protein.
B) disrupts the secondary, tertiary, or quaternary structure of a protein.
C) is always irreversible.
D) hydrolyzes peptide bonds.
E) can only occur in a protein with quaternary structure.
Answer: B
Objective: 19.6
53) One heavy metal that can cause denaturation of a protein is

A) silver.
B) sodium.
C) barium.
D) iron.
E) calcium.
Answer: A
Objective: 19.6
54) Heavy metals denature proteins by

A) releasing amino acids.
B) disrupting hydrophobic interactions.
C) changing the pH of the protein solution.
D) changing the temperature of the protein solution.
E) disrupting disulfide bonds.
Answer: E
Objective: 19.6
55) An acid can denature a protein by

A) agitating the protein chains.
B) disrupting hydrogen bonds between R groups chains.
C) disrupting hydrophobic interactions within a protein chain.
D) removing helping molecules such as heme.
E) breaking disulfide bridges.
Answer: B
Objective: 19.6
16
19.2 Bimodal Questions
1) Immunoglobulin, a protein that stimulates immune responses, would be classified as a ________

protein.
A) transport
B) structural
C) storage
D) protection
E) catalytic
Answer: D
Objective: 19.1
2) What amino acids have polar R groups that are attracted to water?
A) hydrophilic
B) hydrophobic
C) nonpolar
D) aromatic
E) hydrocarbon
Answer: A
Objective: 19.1
3) At what pH would you expect valine, an amino acid with a neutral R group, to be in the zwitterionic
form?
A) 1
B) 4
C) 6
D) 10
E) 14
Answer: C
Objective: 19.2
17
4) Consider the R groups of the following amino acids:
cysteine: -CH2SH; alanine: -CH3; serine: -CH2OH
The name for the dipeptide shown below is ________.
CH3 O CH2OH
| |
NH2 C H - C - NH C HCOOH
A) alanyl-cysteine
B) alanyl-serine
C) seryl-alanine
D) seryl-cysteine
E) serine-alanine
Answer: B
Objective: 19.3
5) The peptide hormone that regulates uterine contractions during labor is ________.
A) oxytocin
B) vasopressin
C) myoglobin
D) an endorphin
E) an enkephalin
Answer: A
Objective: 19.4
6) In an enzyme, the polypeptide chain folds into a compact shape known as the ________ structure.
A) pleated
B) primary
C) secondary
D) tertiary
E) quaternary
Answer: D
Objective: 19.5
7) When two protein chains combine to form an active protein, the structural level is ________.
A) pleated
B) primary
C) secondary
D) tertiary
E) quaternary
Answer: E
Objective: 19.5
18
8) Hydrophobic interactions help to stabilize the ________ structure(s) of a protein.
A) primary
B) secondary
C) secondary and tertiary
D) tertiary and quaternary
E) secondary and quaternary
Answer: D
Objective: 19.5
9) What process occurs when heat, acids, bases, and heavy metal ions cause a loss of biological function of
a protein?
A) denaturation
B) saponification
C) hydrogenation
D) amidation
E) esterification
Answer: A
Objective: 19.6
10) In digestion, proteins are broken down into amino acids by a(n) ________ reaction.
A) saponification
B) reduction
C) hydrolysis
D) oxidation
E) denaturation
Answer: C
Objective: 19.6
19.3 Short Answer Questions
1) Collagen can be classified as a ________ protein.

Answer: structural
Objective: 19.1
2) The protein that transports oxygen in the blood is ________.

Answer: hemoglobin
Objective: 19.1
3) Proteins that stimulate immune response are known as ________.

Answer: immunoglobulins
Objective: 19.1
19
4) Amino acids that are not synthesized in the body but must be ingested with the diet are called
________ amino acids.
Answer: essential
Objective: 19.1
5) A zwitterion of any amino acid has a net charge of ________.

Answer: zero
Objective: 19.2
6) The isoelectric point for any amino acid is the pH at which the amino acid has a net charge of ________.
Answer: zero
Objective: 19.2
7) Electrophoresis is a laboratory technique for separating amino acids using their different ________.
Answer: isoelectric points
Objective: 19.2
8) Write the zwitterion of glycine.

Answer:
Objective: 19.2
9) Circle the peptide bond in this structure.
Answer:
Objective: 19.3
20
19.4 True/False
1) Hemoglobin is a transport protein.

Answer: TRUE
Objective: 19.1
2) Insulin is a transport protein.

Answer: FALSE
Objective: 19.1
3) Zwitterions have an overall positive charge.

Answer: FALSE
Objective: 19.2
4) The dipeptide abbreviated as Gly-Lys is the same as the dipeptide abbreviated as Lys-Gly.
Answer: FALSE
Objective: 19.3
5) Sickle-cell anemia is caused by a change in the primary structure of a subunit of the hemoglobin
protein.
Answer: TRUE
Objective: 19.4
6) The peptide sequence Gly-Gly-Gly gives the primary structure of a tripeptide.

Answer: TRUE
Objective: 19.4
7) Disulfide bonds stabilize the tertiary structure of a protein.

Answer: TRUE
Objective: 19.5
8) Lysine and glutamic acid form hydrophobic interactions.

Answer: FALSE
Objective: 19.5
9) Upon hydrolysis the dipeptide abbreviated as Gly-Lys will yield the same products as the dipeptide
abbreviated as Lys-Gly.
Answer: TRUE
Objective: 19.6
21
10) Lead ions disrupt hydrophobic interactions.
Answer: FALSE
Objective: 19.6
19.5 Matching Questions
Identify the structural level in each protein.
A) quaternary
B) tertiary
C) secondary structure
D) primary structure
1) The protein folds into a compact structure stabilized by interactions between R groups.
Objective: 19.4, 19.5
2) the combination of two or more protein molecules to form an active protein

3) pleated sheet
4) the peptide bonds between the amino acids

5) the structural level achieved when hydrogen bonds form between the carboxyl group of one amino
acid and the amino group of a different amino acid
Answers: 1) B 2) A 3) C 4) D 5) C
22
Classify each protein by function.
A) contractile
B) structural
C) catalytic
D) protection
E) transport
6) trypsin for the hydrolysis of protein

Objective: 19.1
7) lipoproteins in the blood

Objective: 19.1
8) collagen in tendons and cartilage

Objective: 19.1
9) antibodies
Objective: 19.1
10) actin in muscle

Objective: 19.1
Answers: 6) C 7) E 8) B 9) D 10) A
23
Would an amino acid with the given R group be most likely to be found in the hydrophobic or hydrophilic region of
a protein?
A) both
B) hydrophilic
C) hydrophobic
11) -CH2 - CH - CH3

|
CH3
Objective: 19.5
12) - CH - CH3
|
OH
Objective: 19.5
13) - CH3
Objective: 19.5
14) -CH2CH2SCH3
Objective: 19.5
15) O
-CH2 - C - NH2
Objective: 19.5
16)
Objective: 19.5
24
17)
Objective: 19.5
18) -CH - CH2 - CH3

|
CH3
Objective: 19.5
19)
Objective: 19.5
Answers: 11) C 12) B 13) C 14) C 15) B 16) B 17) B 18) C 19) C
25

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Chapter 19

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General, Organic & Biological Chemistry, 5e (Timberlake)

Chapter 19 Amino Acids and Proteins

19.1 Multiple-Choice Questions

1) Which of the following is NOT a function of proteins?

3) Wool is primarily made up of

6) The following amino acid R group chain is

11) Glycine is the only naturally occurring amino acid that is

12) The side chain for histidine is classified as a ________ R group.

13) A basic amino acid has an R group that contains

15) At a pH < 5, the zwitterion for alanine (pI = 6) will have

19) In a typical amino acid zwitterion, the carboxylate end is

Ala: -CH3; Ser: -CH2OH; Asp: -CH2COH

24) In the peptide Ala-Try-Gly-Phe, the N-terminal amino acid is

25) In the peptide Ser-Cys-Ala-Gly, the C-terminal end is

28) A peptide bond contains which kind of functional group?

30) Which of the following is an example of a secondary protein structure?

33) Enkephalins are polypeptides that have

34) Enkephalins, naturally produced opiates in the body, are found in

36) Which of the following is a secondary protein structure?

37) The secondary structure of collagen is distinguished by

39) Hemoglobin is an example of a protein with

41) Within hemoglobin, the heme functions as

-CH2 C O- and -CH2CH2CH2CH2NH3+

46) Disulfide bonds in a protein chain connect

48) The function of myoglobin is to

49) In sickle-cell anemia, the hemoglobin molecules

50) Acids and bases denature a protein by disrupting

51) Heat denatures a protein by disrupting

53) One heavy metal that can cause denaturation of a protein is

54) Heavy metals denature proteins by

55) An acid can denature a protein by

1) Immunoglobulin, a protein that stimulates immune responses, would be classified as a ________

19.3 Short Answer Questions

1) Collagen can be classified as a ________ protein.

2) The protein that transports oxygen in the blood is ________.

3) Proteins that stimulate immune response are known as ________.

5) A zwitterion of any amino acid has a net charge of ________.

8) Write the zwitterion of glycine.

9) Circle the peptide bond in this structure.

1) Hemoglobin is a transport protein.

2) Insulin is a transport protein.

3) Zwitterions have an overall positive charge.

6) The peptide sequence Gly-Gly-Gly gives the primary structure of a tripeptide.

7) Disulfide bonds stabilize the tertiary structure of a protein.

8) Lysine and glutamic acid form hydrophobic interactions.

19.5 Matching Questions

Identify the structural level in each protein.

2) the combination of two or more protein molecules to form an active protein

4) the peptide bonds between the amino acids

6) trypsin for the hydrolysis of protein

7) lipoproteins in the blood

8) collagen in tendons and cartilage

10) actin in muscle

11) -CH2 - CH - CH3

18) -CH - CH2 - CH3

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