Chapter 04 - The Three-Dimensional Structure of Proteins

Exhibit 4A
The following question(s) refer to this peptide:

Cys-Ala-Gly-Arg-Gln-Met

1. Refer to Exhibit 4A. The amino terminal amino acid is:

a. Arg
b. Cys
c. Gln
d. Met
e. None of these.

2. Refer to Exhibit 4A. The overall, net ionic charge on this peptide at pH = 7 would be:
a. +2
b. +1
c. 0
d. −1
e. −2

3. Hydrogen bonds are most important in this type of structure in proteins:

a. primary structure
b. secondary structure
c. tertiary structure
d. quaternary structure
e. All of these

4. The location of prosthetic groups is shown in this level of structure:

a. primary structure
b. secondary structure
c. tertiary structure
d. quaternary structure
e. All of these

5. Covalent bonds are important in all these structures, except:

a. primary structure
b. secondary structure
c. tertiary structure
d. quaternary structure
e. All of these

6. Which of the following forces are involved in maintaining the primary structure of a protein?
a. covalent bonds
b. hydrogen bonds
c. ionic interactions
d. hydrophobic interactions

7. A single amino substitution can give rise to a malfunctioning protein.

a. True
b. False

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Chapter 04 - The Three-Dimensional Structure of Proteins

8. What happens when a protein is denatured?

a. Its secondary structure is disrupted but its primary structure remains intact.
b. Its primary structure is disrupted but its secondary structure remains intact.
c. It is broken apart into its constituent amino acids.
d. It becomes all α-helix.

9. Which of the following amino acids is unlikely to be found in an α-helix?

a. phenylalanine
b. tryptophan
c. proline
d. lysine

10. Which of the following factors tend to destabilize α-helices?

a. clusters of amino acids with bulky R-groups
b. clusters of amino acids with similarly charged R-groups
c. Both of these.
d. Neither of these

11. Which of the following is true?

a. The peptide bonds in the β-sheet are extended.
b. The peptide bonds in the α-helix coil back on themselves.
c. Both α-helices and β-sheets can be found as part of tertiary structure.
d. All of these

12. Which of the following best describes a motif?

a. a repetitive supersecondary structure
b. a common nonrepetitive irregularity found in antiparallel β-sheets
c. a protein conformation with biological activity
d. a group of atoms other than an amino acid

13. Which of the following is the most common function for fibrous proteins?
a. enzymes
b. structural roles.
c. carrier molecules.
d. enzymes and carrier molecules.
e. All of these.

14. Which one is not an example of supersecondary structure?

a. the pyrrole ring
b. the Greek key
c. the β-meander
d. the β-barrel

15. As an animal ages, the amount of cross-linking of collagen in tissue

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Chapter 04 - The Three-Dimensional Structure of Proteins

a. tends to decrease.
b. tends to increase.
c. tends to remain unchanged.

16. The following is true about the hydroxyproline in collagen:

a. Hydroxyproline is incorporated into the chain during polymerization of amino acids.
b. Vitamin C is necessary for the synthesis of hydroxyproline.
c. Hydroxyproline is important in holding the 3 strands of collagen together.
d. Hydroxyproline requires Vitamin C for its synthesis and it holds the collagen helix together.
e. All of these.
17. Fibrous proteins
a. are always composed of helical structures.
b. are always composed of β-sheets.
c. can be composed of either helical or β-sheet structures.
d. are always water soluble

18. Domains are

a. independently folded regions of proteins
b. the α-helical portions of proteins
c. the β-pleated regions of proteins
d. all of the above

19. Which of the following amino acid residues would most likely be found in the interior of a globular protein?
a. glutamic acid
b. lysine
c. leucine
d. serine

20. Disulfide bonds in proteins occur between the side chains of which of the following amino acid residues?
a. glutamine
b. lysine
c. cysteine
d. methionine

Exhibit 4B

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Chapter 04 - The Three-Dimensional Structure of Proteins

21. Refer to Exhibit 4B. The type of bonding labeled "O" in these figure is:
a. Hydrogen bonding of the peptide backbone
b. Covalent bonding involving the R-groups
c. Hydrophobic interactions
d. Metal ion coordination
e. Electrostatic attraction

22. Refer to Exhibit 4B. Which one shows hydrogen bonding of R-groups?
a. M
b. N
c. P
d. M and N
e. All of these

23. Refer to Exhibit 4B. Which one shows covalent bonding of R-groups?
a. K
b. L
c. O
d. K and L
e. All of these

24. X-ray crystallography is used to determine protein structure because

a. it can be done on dilute solutions
b. it requires no calculations
c. the positions of all atoms can be found by this method
d. all of these

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Chapter 04 - The Three-Dimensional Structure of Proteins

25. The tertiary structure of a protein is usually a result of which of the following interactions?
a. intramolecular hydrogen bonding
b. electrostatic interactions
c. hydrophobic interactions
d. all of these

26. Why does myoglobin have a histidine that prevents both O2 and CO from binding perpendicularly to the heme
plane?
a. This increases myoglobin's affinity for O2.
b. This increases myoglobin's affinity for CO.
c. This lessens the difference in myoglobin's affinity for CO versus O2.
d. This prevents the iron of the heme from being oxidized.

27. Which of the following is not true?

a. The heme group of myoglobin is held in place only through non-covalent bonding.
b. The F8 histidine is important to the function of myoglobin
c. The E7 histidine is important to the function of myoglobin
d. Myoglobin and hemoglobin differ only in one amino acid

28. The following bond forces are important in tertiary structure:

a. Disulfide bonds
b. Hydrogen bonds
c. Hydrophobic attraction
d. Both hydrogen bonds and hydrophobic attraction.
e. All of these are important in tertiary structure

29. Which of the following forces are involved in maintaining the quaternary structure of a protein?
a. hydrogen bonds
b. ionic interactions
c. hydrophobic interactions
d. All of these

30. Under normal circumstances:

a. Adult Hb binds to oxygen more tightly than Mb binds.
b. Fetal Hb binds oxygen more tightly than adult Hb.
c. Adult Hb binds oxygen more tightly than either fetal Hb or Mb binds.
d. Mb has the lowest affinity for oxygen of the 3.
e. More than one of these statements is correct.

31. Which of the following is not a characteristic of hemoglobin?

a. It contains two different types of subunits .
b. It contains a prosthetic group.
c. It is an allosteric enzyme.
d. It transports oxygen.
e. All of these statements are true for Hb.

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Chapter 04 - The Three-Dimensional Structure of Proteins

32. In allosteric interactions

a. proteins that consist of a single polypeptide chain form aggregates.
b. disulfide bonds are broken.
c. changes that take place in one site of a protein cause changes at a distant site.
d. metal ions always bind to the protein.

33. Which of the following best describes what happens when hemoglobin binds bisphosphoglyceric acid (BPG)?
a. Binding of BPG leads to tighter binding of oxygen.
b. Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb.
c. Binding of BPG is important to the allosteric nature of hemoglobin
d. Binding of BPG causes the subunits of hemoglobin to separate.

34. In the Bohr effect the binding of oxygen to hemoglobin

a. is increased by the presence of Na+
b. is increased by the presence of H+ and CO2
c. is decreased by the presence of H+ and CO2
d. is unchanged

35. Variations in the structure of hemoglobin

a. do not always have an adverse effect on health
b. can alter the binding of heme to the protein
c. can occur on the surface of the protein
d. all of these

36. What would happen to hemoglobin if the BPG were removed?

a. It would not bind oxygen
b. It would dissociate into monomers
c. its oxygen binding curve would resemble that of myoglobin
d. all of the choices

37. Adult hemoglobin is half saturated with oxygen at what partial pressure of oxygen?
a. 5 torr
b. 10 torr
c. 25 torr
d. 50 torr
e. 100 torr

38. Hydroxyurea works as a treatment for sickle cell anemia because it

a. causes myoglobin to act like hemoglobin
b. causes the body to produce fetal hemoglobin
c. causes hemoglobin to dissociate into monomers, thereby quadrupling the effective concentration of
oxygen carrying molecules
d. none of the choices
39. What is the major force that drives nonpolar substances out of aqueous solution?

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Chapter 04 - The Three-Dimensional Structure of Proteins

a. Increased enthalpy of hydrophobic bonds formed between solute molecules.

b. Decreased entropy of newly organized solute molecules.
c. Increased entropy of newly organized solute molecules.
d. Increased enthalpy of H-bonds in the solvent water.
e. Increased entropy of solvent water molecules.

40. The information needed for the structure of a protein is contained in

a. amino acid composition
b. primary structure
c. secondary structure
d. tertiary structure

41. Proteins that aid in the correct and timely folding of other proteins are called
a. motifs.
b. chaperones.
c. liposomes.
d. cooperative.

42. The three-dimensional shapes of proteins with biological activities are called _____.
a. prosthetic groups
b. subunits
c. native conformations
d. domains

43. The order in which the amino acids in a protein are linked by peptide bonds a. Primary structure
b. Secondary structure
c. Domains
d. Tertiary structure
e. Quaternary structure

44. Specific clusters of secondary structural motifs in proteins

a. Primary structure
b. Secondary structure
c. Domains
d. Tertiary structure
e. Quaternary structure

45. The interaction of several polypeptide chains in a multisubunit protein a. Primary structure
b. Secondary structure
c. Domains
d. Tertiary structure
e. Quaternary structure

46. _____ are spherical aggregates of lipids arranged so that the polar head groups are in contact with water and
the nonpolar tails are sequestered from water.
a. Liposomes
b. Azotosomes
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Chapter 04 - The Three-Dimensional Structure of Proteins

c. Escheriosomes
d. Chromosomes

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