Deck 19: Amino Acids and Proteins
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Deck 19: Amino Acids and Proteins
1
Wool is primarily made up of
A) protein.
B) carbohydrate.
C) globin.
D) triacylglycerols.
E) enkephalin.
A) protein.
B) carbohydrate.
C) globin.
D) triacylglycerols.
E) enkephalin.
protein.
2
The side chain for histidine is classified as a __________ R group.
A) basic
B) neutral
C) acidic
D) nonpolar
E) polar
A) basic
B) neutral
C) acidic
D) nonpolar
E) polar
basic
3
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.
A) an amine group.
B) a carboxyl group.
C) a methyl group.
D) an alcohol group.
E) a thiol group.
an amine group.
4
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.
A) essential.
B) polar.
C) nonpolar.
D) complete.
E) incomplete.
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5
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
A) eggs
B) milk
C) beans
D) steak
E) ham
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6
The following amino acid R group chain is 
A) polar.
B) hydrophobic.
C) hydrophilic.
D) acidic.
E) basic.

A) polar.
B) hydrophobic.
C) hydrophilic.
D) acidic.
E) basic.
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7
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
A) Lysine
B) Tyrosine
C) Glutamic acid
D) All of the amino acids
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8
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.
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.
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9
The R group for serine is -CH₂OH. As a zwitterion, serine has the structural formula
A)
B)
C)
D)
E)
A)

B)

C)

D)

E)

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10
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
A) Lysine
B) Tyrosine
C) Glutamic acid
D) All of the amino acids
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11
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
A) transport
B) hormonal
C) catalytic
D) structural
E) contractile
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12
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
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
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13
Collagen, a protein found in tendons and cartilage, would be classified as a __________ protein.
A) catalytic
B) structural
C) transport
D) storage
E) hormone
A) catalytic
B) structural
C) transport
D) storage
E) hormone
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14
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.
A) carboxyl group.
B) alpha carbon.
C) amino group.
D) side (R) group.
E) hydrogen bonding.
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15
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.
A) positively charged.
B) negatively charged.
C) neutral.
D) soluble in a nonpolar solvent.
E) attached to an amine.
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16
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.
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.
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17
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.
A) a sulfur atom.
B) a chlorine atom.
C) a sodium atom.
D) a phenyl ring.
E) a heterocyclic ring.
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18
What is the structural formula of glutamic acid (pI = 3.2) at pH = 1?
A)
B)
C)
D)
E)
A)

B)

C)

D)

E)

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19
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.
A) negatively charged.
B) positively charged.
C) neutral.
D) in the L- form.
E) achiral.
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20
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.
A) wheat and rice.
B) rice and beans.
C) almonds and walnuts.
D) corn and beans.
E) wheat and corn.
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21
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.
A) ester bonds.
B) ether bonds.
C) amide bonds.
D) glycosidic bonds.
E) sulfide bonds.
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22
Which of the following functional groups of an amino acid would be in the ionized state at high pH?
A)
B) -CH?OH
C) -CH3
D)
E)
A)
B) -CH?OH
C) -CH3
D)
E)

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23
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.
A) hydrogen bonds.
B) hydrophobic interactions.
C) disulfide bonds.
D) salt bridges.
E) peptide bonds.
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24
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.
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.
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25
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.
A) peptide.
B) protein.
C) enzyme.
D) globulin.
E) hormone.
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26
Which of the following is the correct structure for Ser-Ala-Asp? The appropriate side chains look like this. Ala: - CH3; Ser: - CH?OH; Asp:
A)
B)
C)
D)
E)
A)

B)

C)

D)

E)

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27
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
A) dipeptide
B) triglyceride
C) a helix
D) amino acid
E) fatty acid
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28
In the peptide Ala-Try-Gly-Phe, the N-terminal amino acid is
A) alanine.
B) phenylalanine.
C) tryptophan.
D) aspartic acid.
E) glycine.
A) alanine.
B) phenylalanine.
C) tryptophan.
D) aspartic acid.
E) glycine.
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29
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
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
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30
Enkephalins are polypeptides that have
A) a sweet taste.
B) a bitter taste.
C) extra caloric value.
D) pain-killing properties.
E) hormone activity.
A) a sweet taste.
B) a bitter taste.
C) extra caloric value.
D) pain-killing properties.
E) hormone activity.
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31
A peptide bond contains which kind of functional group?
A) alcohol
B) amine
C) amide
D) carboxylic acid
E) ketone
A) alcohol
B) amine
C) amide
D) carboxylic acid
E) ketone
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32
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
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
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33
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
A) hydrogen bonds
B) disulfide bridges
C) salt bridges
D) hydrophilic interactions
E) hydrophobic interactions
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34
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.
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.
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35
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.
A) disulfide bridges.
B) hydrogen bonds.
C) salt bridges.
D) a prosthetic group.
E) a β-pleated sheet.
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36
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.
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.
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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.
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.
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38
Which of the following is a secondary protein structure?
A) α helix
B) Ser-Met-Ala-Gly-Ile
C) disulfide bond
D) salt bridges
E) hydrophobic interactions
A) α helix
B) Ser-Met-Ala-Gly-Ile
C) disulfide bond
D) salt bridges
E) hydrophobic interactions
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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.
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.
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40
In the peptide Ser-Cys-Ala-Gly, the C-terminal end is
A) serine.
B) serotonin.
C) glycine.
D) glycerine.
E) alanine.
A) serine.
B) serotonin.
C) glycine.
D) glycerine.
E) alanine.
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41
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.
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.
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42
The peptide hormone that regulates uterine contractions during labor is __________.
A) oxytocin
B) vasopressin
C) myoglobin
D) an endorphin
E) an enkephalin
A) oxytocin
B) vasopressin
C) myoglobin
D) an endorphin
E) an enkephalin
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43
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.
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.
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44
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.
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.
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45
What type of interaction would you expect between the following R groups in the tertiary structure of a protein? 
A) disulfide bonds
B) salt bridges
C) hydrogen bonds
D) hydrophobic interactions
E) peptide bonds

A) disulfide bonds
B) salt bridges
C) hydrogen bonds
D) hydrophobic interactions
E) peptide bonds
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46
The fibrous protein responsible for the structure of hair and wool is
A) keratin.
B) collagen.
C) endorphin.
D) myosin.
E) casein.
A) keratin.
B) collagen.
C) endorphin.
D) myosin.
E) casein.
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47
One heavy metal that can cause denaturation of a protein is
A) silver.
B) sodium.
C) barium.
D) iron.
E) calcium.
A) silver.
B) sodium.
C) barium.
D) iron.
E) calcium.
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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.
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.
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49
Consider the R groups of the following amino acids: cysteine: -CH₂SH; alanine: - 3CH3; serine: -CH₂OH
The name for the dipeptide shown below is __________.
A) alanyl-cysteine
B) alanyl-serine
C) seryl-alanine
D) seryl-cysteine
E) serine-alanine
The name for the dipeptide shown below is __________.

A) alanyl-cysteine
B) alanyl-serine
C) seryl-alanine
D) seryl-cysteine
E) serine-alanine
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50
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.
A) a disulfide bridge.
B) an oxygen carrier.
C) a reducing agent.
D) an α subunit.
E) one of the four protein subunits.
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51
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.
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.
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52
Hemoglobin has a total of __________ protein chains in its quaternary structure.
A) one
B) two
C) three
D) four
E) five
A) one
B) two
C) three
D) four
E) five
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53
What kinds of interactions are NOT part of tertiary protein structure?
A) peptide bonds
B) disulfide bonds
C) hydrophilic interactions
D) salt bridges
E) hydrophobic interactions
A) peptide bonds
B) disulfide bonds
C) hydrophilic interactions
D) salt bridges
E) hydrophobic interactions
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54
Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?
A) -CH?OH
B) - CH?COO-
C)
D) - CH?CH?CH?CH? H3
E)
A) -CH?OH
B) - CH?COO-
C)

D) - CH?CH?CH?CH? H3
E)
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55
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) 7
D) 10
E) 14
A) 1
B) 4
C) 7
D) 10
E) 14
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56
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.
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.
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57
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.
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.
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58
What amino acids have polar R groups that are attracted to water?
A) hydrophilic
B) hydrophobic
C) nonpolar
D) aromatic
E) hydrocarbon
A) hydrophilic
B) hydrophobic
C) nonpolar
D) aromatic
E) hydrocarbon
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59
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.
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.
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60
Immunoglobulin, a protein that stimulates immune responses, would be classified as a __________ protein.
A) transport
B) structural
C) storage
D) protection
E) catalytic
A) transport
B) structural
C) storage
D) protection
E) catalytic
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61
The protein that transports oxygen in the blood is __________.
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62
The isoelectric point for any amino acid is the pH at which the amino acid has a net charge of __________.
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63
Insulin is a transport protein.
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64
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
A) pleated
B) primary
C) secondary
D) tertiary
E) quaternary
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65
Hemoglobin is a transport protein.
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66
The dipeptide abbreviated as Gly-Lys is the same as the dipeptide abbreviated as Lys-Gly.
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67
Electrophoresis is a laboratory technique for separating amino acids using their different __________.
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68
In digestion, proteins are broken down into amino acids by a(n) __________ reaction.
A) saponification
B) reduction
C) hydrolysis
D) oxidation
E) denaturation
A) saponification
B) reduction
C) hydrolysis
D) oxidation
E) denaturation
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69
When two protein chains combine to form an active protein, the structural level is __________.
A) pleated
B) primary
C) secondary
D) tertiary
E) quaternary
A) pleated
B) primary
C) secondary
D) tertiary
E) quaternary
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70
Amino acids that are not synthesized in the body but must be ingested with the diet are called __________ amino acids.
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71
Proteins that stimulate immune response are known as __________.
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72
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
A) denaturation
B) saponification
C) hydrogenation
D) amidation
E) esterification
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73
Sickle-cell anemia is caused by a change in the primary structure of a subunit of the hemoglobin protein.
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74
A zwitterion of any amino acid has a net charge of __________.
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75
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
A) primary
B) secondary
C) secondary and tertiary
D) tertiary and quaternary
E) secondary and quaternary
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76
Zwitterions have an overall positive charge.
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77
The peptide sequence Gly-Gly-Gly gives the primary structure of a tripeptide.
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78
Write the zwitterion of glycine.
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79
Circle the peptide bond in this structure. 

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80
Collagen can be classified as a __________ protein.
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