Lehninger Principles of Biochemistry Test Bank CH 4

Chapter 4 The Three-Dimensional Structure of Proteins
Multiple Choice Questions

1. Overview of protein structure
Pages: 117−118 Difficulty: 1 Ans: D
All of the following are considered “weak” interactions in proteins, except:
A) hydrogen bonds.
B) hydrophobic interactions.
C) ionic bonds.
D) peptide bonds.
E) van der Waals forces.

Pages: 117−118 Difficulty: 2 Ans: A
The most important contribution to the stability of a protein’s conformation appears to be the:
A) entropy increase from the decrease in ordered water molecules forming a solvent shell around it.
B) maximum entropy increase from ionic interactions between the ionized amino acids in a protein.
C) sum of free energies of formation of many weak interactions among the hundreds of amino acids
in a protein.
D) sum of free energies of formation of many weak interactions between its polar amino acids and
surrounding water.
E) stabilizing effect of hydrogen bonding between the carbonyl group of one peptide bond and the
amino group of another.

Page: 118 Difficulty: 1 Ans: D
In an aqueous solution, protein conformation is determined by two major factors. One is the
formation of the maximum number of hydrogen bonds. The other is the:
A) formation of the maximum number of hydrophilic interactions.

B) maximization of ionic interactions.
C) minimization of entropy by the formation of a water solvent shell around the protein.
D) placement of hydrophobic amino acid residues within the interior of the protein.
E) placement of polar amino acid residues around the exterior of the protein.

Page: 118 Difficulty: 2 Ans: B
Pauling and Corey’s studies of the peptide bond showed that:
A) at pH 7, many different peptide bond conformations are equally probable.

B) peptide bonds are essentially planar, with no rotation about the C—N axis.
C) peptide bonds in proteins are unusual, and unlike those in small model compounds.
D) peptide bond structure is extraordinarily complex.
E) primary structure of all proteins is similar, although the secondary and tertiary structure may
differ greatly.
Chapter 4 The Three-Dimensional Structure of Proteins 39

Page: 119 Difficulty: 3 Ans: A
In the diagram below, the plane drawn behind the peptide bond indicates the:
A) absence of rotation around the C—N bond because of its partial double-bond character.
B) plane of rotation around the Cα—N bond.
C) region of steric hindrance determined by the large C=O group.
D) region of the peptide bond that contributes to a Ramachandran plot.
E) theoretical space between –180 and +180 degrees that can be occupied by the φ and ψ angles in
the peptide bond.

Which of the following best represents the backbone arrangement of two peptide bonds?
A) Cα—N—Cα—C—Cα—N—Cα—C
B) Cα—N—C—C—N—Cα
C) C—N—Cα—Cα—C—N
D) Cα—C—N—Cα—C—N
E) Cα—Cα—C—N—Cα—Cα—C

Which of the following pairs of bonds within a peptide backbone show free rotation around both bonds?
A) Cα—C and N—Cα

B) C=O and N—C
C) C=O and N—Cα
D) N—C and Cα—C
E) N—Cα and N—C
8. Protein secondary structure

In the α helix the hydrogen bonds:
A) are roughly parallel to the axis of the helix.

B) are roughly perpendicular to the axis of the helix.
C) occur mainly between electronegative atoms of the R groups.
D) occur only between some of the amino acids of the helix.
E) occur only near the amino and carboxyl termini of the helix.
40 Chapter 4 The Three-Dimensional Structure of Proteins

In an α helix, the R groups on the amino acid residues:
A) alternate between the outside and the inside of the helix.

B) are found on the outside of the helix spiral.
C) cause only right-handed helices to form.
D) generate the hydrogen bonds that form the helix.
E) stack within the interior of the helix.

Thr and/or Leu residues tend to disrupt an α helix when they occur next to each other in a protein because:
A) an amino acids like Thr is highly hydrophobic.

B) covalent interactions may occur between the Thr side chains.
C) electrostatic repulsion occurs between the Thr side chains.
D) steric hindrance occurs between the bulky Thr side chains.
E) the R group of Thr can form a hydrogen bond.

A D-amino acid would interrupt an α helix made of L-amino acids. Another naturally occurring
hindrance to the formation of an α helix is the presence of:
A) a negatively charged Arg residue.

B) a nonpolar residue near the carboxyl terminus.
C) a positively charged Lys residue.
D) a Pro residue.
E) two Ala residues side by side.

Page: 122 Difficulty: 3 Ans: E
An α helix would be destabilized most by:
A) an electric dipole spanning several peptide bonds throughout the α helix.

B) interactions between neighboring Asp and Arg residues.
C) interactions between two adjacent hydrophobic Val residues.
D) the presence of an Arg residue near the carboxyl terminus of the α helix.
E) the presence of two Lys residues near the amino terminus of the α helix.

The major reason that antiparallel β-stranded protein structures are more stable than parallel β-
stranded structures is that the latter:
A) are in a slightly less extended configuration than antiparallel strands.

B) do not have as many disulfide crosslinks between adjacent strands.
C) do not stack in sheets as well as antiparallel strands.
D) have fewer lateral hydrogen bonds than antiparallel strands.
E) have weaker hydrogen bonds laterally between adjacent strands.

Page: 124 Difficulty: 1 Ans: C
Amino acid residues commonly found in the middle of β turn are:
A) Ala and Gly.

B) hydrophobic.
C) Pro and Gly.
D) those with ionized R-groups.
E) two Cys.

A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-Gly-. The sequence is
most probably part of a(n):
A) antiparallel β sheet.
B) parallel β sheet.
C) α helix.
D) α sheet.
E) β turn.
16. Protein tertiary and quaternary structures

The three-dimensional conformation of a protein may be strongly influenced by amino acid residues
that are very far apart in sequence. This relationship is in contrast to secondary structure, where the
amino acid residues are:
A) always side by side.

B) generally near each other in sequence.
C) invariably restricted to about 7 of the 20 standard amino acids.
D) often on different polypeptide strands.
E) usually near the polypeptide chain’s amino terminus or carboxyl terminus.

The α-keratin chains indicated by the diagram below have undergone one chemical step. To alter the
shape of the α-keratin chains—as in hair waving—what subsequent steps are required?
A) Chemical oxidation and then shape remodeling

B) Chemical reduction and then chemical oxidation
C) Chemical reduction and then shape remodeling
D) Shape remodeling and then chemical oxidation
E) Shape remodeling and then chemical reduction

Which of the following statements is false?
A) Collagen is a protein in which the polypeptides are mainly in the α-helix conformation.
B) Disulfide linkages are important for keratin structure.
C) Gly residues are particularly abundant in collagen.
D) Silk fibroin is a protein in which the polypeptide is almost entirely in the β conformation.
E) α-keratin is a protein in which the polypeptides are mainly in the α-helix conformation.

Kendrew’s studies of the globular myoglobin structure demonstrated that:
A) “corners” between α-helical regions invariably lacked proline residue.

B) highly polar or charged amino acid residues tended to be located interiorally.
C) myoglobin was completely different from hemoglobin, as expected.
D) the structure was very compact, with virtually no internal space available for water.
E) the α helix predicted by Pauling and Corey was not found in myoglobin.

Pages: 136−137 Difficulty: 1 Ans: E
Determining the precise spacing of atoms within a large protein is possible only through the use of:
A) electron microscopy.
B) light microscopy.
C) molecular model building.
D) Ramachandran plots.
E) x-ray diffraction.

Proteins often have regions that show specific, coherent patterns of folding or function. These
regions are called:
A) domains.
B) oligomers.
C) peptides.
D) sites.
E) subunits.

Which of the following statements concerning protein domains is true?
A) They are a form of secondary structure.

B) They are examples of structural motifs.
C) They consist of separate polypeptide chains (subunits).
D) They have been found only in prokaryotic proteins.
E) They may retain their correct shape even when separated from the rest of the protein.

The structural classification of proteins (based on motifs) is based primarily on their:
A) amino acid sequence.

B) evolutionary relationships.
C) function.
D) secondary structure content and arrangement.
E) subunit content and arrangement.

Proteins are classified within families or superfamilies based on similarities in:
A) evolutionary origin.
B) physico-chemical properties.
C) structure and/or function.
D) subcellular location.
E) subunit structure.

Which of the following statements about oligomeric proteins is false?
A) A subunit may be similar to other proteins.

B) All subunits must be identical.
C) Many have regulatory roles.
D) Some oligomeric proteins can further associate into large fibers.
E) Some subunits may have nonprotein prosthetic groups.

A repeating structural unit in a multimeric protein is known as a(n):
A) domain.
B) motif.
C) oligomer.
D) protomer.
E) subunit.

Page: 144−146 Difficulty: 2 Ans: A
Which of the following statements concerning rotational symmetry in proteins is false?
A) It involves rotation of proteins inside the cell.

B) It is frequently seen in the subunits of oligomeric proteins.
C) It is frequently seen in viruses.
D) It may involve rotation about one or more axes.
E) It results in closed, packed structures.
28. Protein denaturation and folding

An average protein will not be denatured by:
A) a detergent such as sodium dodecyl sulfate.

B) heating to 90°C.
C) iodoacetic acid.
D) pH 10.
E) urea.

Which of the following is least likely to result in protein denaturation?
A) Altering net charge by changing pH

B) Changing the salt concentration
C) Disruption of weak interactions by boiling
D) Exposure to detergents
E) Mixing with organic solvents such as acetone

Experiments on denaturation and renaturation after the reduction and reoxidation of the —S—S—
bonds in the enzyme ribonuclease (RNase) have shown that:
A) folding of denatured RNase into the native, active conformation, requires the input of energy in
the form of heat.
B) native ribonuclease does not have a unique secondary and tertiary structure.
C) the completely unfolded enzyme, with all —S—S— bonds broken, is still enzymatically active.
D) the enzyme, dissolved in water, is thermodynamically stable relative to the mixture of amino
acids whose residues are contained in RNase.
E) the primary sequence of RNase is sufficient to determine its specific secondary and tertiary
structure.

Which of the following statements concerning the process of spontaneous folding of proteins is false?
A) It may be an essentially random process.

B) It may be defective in some human diseases.
C) It may involve a gradually decreasing range of conformational species.
D) It may involve initial formation of a highly compact state.
E) It may involve initial formation of local secondary structure.

Pages: 151−152 Difficulty: 1 Ans: B
Protein S will fold into its native conformation only when protein Q is also present in the solution.
However, protein Q can fold into its native conformation without protein S. Protein Q, therefore,
may function as a ____________ for protein S.
A) ligand
B) molecular chaperone
C) protein precursor
D) structural motif
E) supersecondary structural unit

Which of the following is not known to be involved in the process of assisted folding of proteins?
A) Chaperonins
B) Disulfide interchange
C) Heat shock proteins
D) Peptide bond hydrolysis
E) Peptide bond isomerization
Short Answer Questions

Page: 116 Difficulty: 2
Any given protein is characterized by a unique amino acid sequence (primary structure) and three-
dimensional (tertiary) structure. How are these related?
Ans: The three-dimensional structure is determined by the amino acid sequence. This means that the
amino acid sequence contains all of the information that is required for the polypeptide chain to fold
up into a discrete three-dimensional shape.

Pages: 117, 147 Difficulty: 2
Name four factors (bonds or other forces) that contribute to stabilizing the native structure of a
protein, and describe one condition or reagent that interferes with each type of stabilizing force.
Ans: Among forces that stabilize native protein structures are (a) disulfide bonds, (b) hydrogen
bonds, (c) hydrophobic interactions, and (d) ionic interactions. Agents that interfere with these forces
are (a) mercaptoethanol or dithiothreitol, (b) pH extremes, (c) detergents and urea, and (d) changes in
pH or ionic strength, respectively.

Pages: 117−118 Difficulty: 2
When a polypeptide is in its native conformation, there are weak interactions between its R groups.
However, when it is denatured there are similar interactions between the protein groups and water.
What then accounts for the greater stability of the native conformation?
Ans: In the unfolded polypeptide, there are ordered solvation shells of water around the protein
groups. The number of water molecules involved in such ordered shells is reduced when the protein
folds, resulting in higher entropy. Hence, the lower free energy of the native conformation.

Draw the resonance structure of a peptide bond, and explain why there is no rotation around the
C—N bond.
Ans: The intermediate resonance structure imparts a partial double bond characteristic to the C—N
bond, thereby prohibiting rotation. (See Fig. 4-2, p. 119.)

Pauling and Corey showed that in small peptides, six atoms associated with the peptide bond all lie in
a plane. Draw a dipeptide of two amino acids in trans linkage (side-chains can be shown as —R),
and indicate which six atoms are part of the planar structure of the peptide bond.
Ans: The N and H of the amino and the C and O of the carbonyl are all in the same plane with the
two Cα atoms, which are diagonally opposite relative to the C—N bond. (See Fig. 4-2, p. 119.)

Draw the hydrogen bonding typically found between two residues in an α helix.
Ans: Hydrogen bonds occur between every carbonyl oxygen in the polypeptide backbone and the
peptide —NH of the fourth amino acid residue toward the amino terminus of the chain. (See Fig. 4-2,
p. 119.)

Describe three of the important features of the α-helical polypeptide structure predicted by Pauling
and Corey. Provide one or two sentences for each feature.
Ans: The α-helical structure of a polypeptide is tightly wound around a long central axis; each turn of
the right-handed helix contains 3.6 residues and stretches 5.4 Å along the axis. The peptide NH is
hydrogen-bonded to the carbonyl oxygen of the fourth amino acid along the sequence toward the
amino terminus. The R groups of the amino acid residues protrude outward from the helical
backbone.

Describe three of the important features of a β sheet polypeptide structure. Provide one or two
sentences for each feature.
Ans: In the β sheet structure, several extended polypeptides, or two regions of the same polypeptide,
lie side by side and are stabilized by hydrogen bonding between adjacent chains. Adjacent chains
may be either parallel (with a repeat distance of about 6.5 Å) or antiparallel (7 Å repeat). The R
groups are often small and alternately protrude from opposite faces of the β sheet.

Why are glycine and proline often found within a β turn?
Ans: A β turn results in a tight 180° reversal in the direction of the polypeptide chain. Glycine is the
smallest and thus most flexible amino acid, and proline can readily assume the cis configuration,
which facilitates a tight turn.

In superhelical proteins, such as collagen, several polypeptide helices are intertwined. What is the
function of this superhelical twisting?
Ans: The superhelical twisting of multiple polypeptide helices makes the overall structure more
compact and increases its overall strength.

Why is silk fibroin so strong, but at the same time so soft and flexible?
Ans: Unlike collagen and keratin, silk fibroin has no covalent crosslinks between adjacent strands, or
between its stacked sheets, making it very flexible. Fibroin’s unusual tensile strength derives from
the fact that the peptide backbone of antiparallel β-strands is fully extended, and that the R-groups in
the stacked pleated sheets interdigitate, preventing any longitudinal sliding of the sheets across one
another.

What is typically found in the interior of a water-soluble globular protein?
Ans: Hydrophobic amino acid residues cluster away from the surface in globular proteins, so much of
the protein’s interior is a tightly packed combination of hydrocarbon and aromatic ring R groups with
very few water molecules.

How does one determine the three-dimensional structure of a protein? Your answer should be more
than the name of a technique.
Ans: The protein is crystallized, and the crystal structure is determined by x-ray diffraction. The
pattern of diffracted x-rays yields, by Fourier transformation, the three-dimensional distribution of
electron density. By matching electron density with the known sequence of amino acids in the
protein, each region of electron density is identified as a single atom. Sometimes, the three-
dimensional structure of a small protein or peptide can be determined in solution by sophisticated
analysis of the NMR spectrum of the polypeptide. This technique can also reveal dynamic aspects of
protein structure such as conformational changes. Computer analysis of two-dimensional NMR
spectra can be used to generate a picture of the three-dimensional structure of a protein.

Page: 136-137 Difficulty: 2
Describe a reservation about the use of x-ray crystallography in determining the three-dimensional
structures of biological molecules.
Ans: To obtain an x-ray picture of a biomolecule, the molecule must be purified and crystallized
under laboratory conditions far different from those encountered by the native molecule.
Biomolecules in the cell also have more flexibility and freedom of motion than can be accommodated
in a rigid crystal structure. Therefore, the static picture obtained from an x-ray analysis of a crystal
may not provide a complete or accurate representation of the biomolecule in vivo.

Explain what is meant by motifs in protein structure.
Ans: Motifs are particularly stable arrangements of elements of secondary structure (e.g., α helix and
β conformation), including the connections between them, which are found in a variety of proteins.

Draw a βαβ loop, and describe what is found in the interior of the loop.
Ans: Hydrophobic amino acid residues are usually found in the interior of the loop; these help
stabilize the arrangement through hydrophobic interactions. (See Fig. 4-20, p. 140.)

Describe the quaternary structure of hemoglobin.
Ans: Each protein molecule is composed of two copies each of two different subunits α and β. The
two αβ protomers are arranged with C2 symmetry.

Describe briefly the two major types of symmetry found in oligomeric proteins and give an example
of each.
Ans: 1) Rotational: In rotational symmetry, subunits are superimposable after rotation about one or
more of the axes. Some examples are hemoglobin and thepoliovirus capsid. 2) Helical: In helical
symmetry, subunits are superimposable after a helical rotation. Some examples are actin filaments
and the tobacco mosaic virus capsid.

What is the rationale for many large proteins containing multiple copies of a polypeptide subunit?
Ans: Each different polypeptide requires a separate gene that must be replicated and transcribed. It is
therefore more efficient to have fewer genes, encoding shorter polypeptides that can be used to
construct many large proteins.

Explain (succinctly) the theoretical and/or experimental arguments in support of this statement: “The
primary sequence of a protein determines its three-dimensional shape and thus its function.”
Ans: Anfinsen showed that a completely denatured enzyme (ribonuclease) could fold spontaneously
into its native, enzymatically active form with only the primary sequence to guide it.

Each of the following reagents or conditions will denature a protein. For each, describe in one or two
sentences what the reagent/condition does to destroy native protein structure.
(a) urea
(b) high temperature
(c) detergent
(d) low pH
Ans: (a) Urea acts primarily by disrupting hydrophobic interactions. (b) High temperature provides
thermal energy greater than the strength of the weak interactions (hydrogen bonds, electrostatic
interactions, hydrophobic interactions, and van der Waals forces, breaking these interactions. (c)
Detergents bind to hydrophobic regions of the protein, preventing hydrophobic interactions among
several hydrophobic patches on the native protein. (d) Low pH causes protonation of the side chains
of Asp, Glu, and His, preventing electrostatic interactions.
How can changes in pH alter the conformation of a protein?
Ans: Changes in pH can influence the extent to which certain amino acid side chains (or the amino
and carboxyl termini) are protonated. The result is a change in net charge on the protein, which can
lead to electrostatic attractions or repulsions between different regions of the protein. The final effect
is a change in the protein’s three-dimensional shape or even complete denaturation.

Once a protein has been denatured, how can it be renatured? If renaturation does not occur, what
might be the explanation?
Ans: Because a protein may be denatured through the disruption of hydrogen bonds and hydrophobic
interactions by salts or organic solvents, removal of those conditions will reestablish the original
aqueous environment, often permitting the protein to fold once again into its native conformation. If
the protein does not renature, it may be because the denaturing treatment removed a required
prosthetic group, or because the normal folding pathway requires the presence of a polypeptide chain
binding protein or molecular chaperone. The normal folding pathway could also be mediated by a
larger polypeptide, which is then cleaved (e.g., insulin). Denatured insulin would not refold easily.

What are two mechanisms by which “chaperone” proteins assist in the correct folding of
polypeptides?
Ans: Chaperones protect unfolded polypeptides from aggregation by binding to hydrophobic regions.
They can also provide a microenvironment that promotes correct folding.

Lehninger Principles of Biochemistry Test Bank CH 4

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Chapter 4 The Three-Dimensional Structure of Proteins

Multiple Choice Questions

2. Overview of protein structure

3. Overview of protein structure

A) formation of the maximum number of hydrophilic interactions.

4. Overview of protein structure

A) at pH 7, many different peptide bond conformations are equally probable.

5. Overview of protein structure

6. Overview of protein structure

7. Overview of protein structure

A) Cα—C and N—Cα

8. Protein secondary structure

A) are roughly parallel to the axis of the helix.

9. Protein secondary structure

A) alternate between the outside and the inside of the helix.

10. Protein secondary structure

A) an amino acids like Thr is highly hydrophobic.

11. Protein secondary structure

A) a negatively charged Arg residue.

12. Protein secondary structure

A) an electric dipole spanning several peptide bonds throughout the α helix.

13. Protein secondary structure

A) are in a slightly less extended configuration than antiparallel strands.

14. Protein secondary structure

A) Ala and Gly.

15. Protein secondary structure

16. Protein tertiary and quaternary structures

A) always side by side.

17. Protein tertiary and quaternary structures

A) Chemical oxidation and then shape remodeling

18. Protein tertiary and quaternary structures

19. Protein tertiary and quaternary structures

A) “corners” between α-helical regions invariably lacked proline residue.

20. Protein tertiary and quaternary structures

21. Protein tertiary and quaternary structures

22. Protein tertiary and quaternary structures

A) They are a form of secondary structure.

23. Protein tertiary and quaternary structures

A) amino acid sequence.

24. Protein tertiary and quaternary structures

25. Protein tertiary and quaternary structures

A) A subunit may be similar to other proteins.

26. Protein tertiary and quaternary structures

27. Protein tertiary and quaternary structures

A) It involves rotation of proteins inside the cell.

28. Protein denaturation and folding

A) a detergent such as sodium dodecyl sulfate.

29. Protein denaturation and folding

A) Altering net charge by changing pH

30. Protein denaturation and folding

31. Protein denaturation and folding

A) It may be an essentially random process.

32. Protein denaturation and folding

33. Protein denaturation and folding

Short Answer Questions

35. Overview of protein structure

36. Overview of protein structure

37. Overview of protein structure

38. Overview of protein structure

39. Protein secondary structure

40. Protein secondary structure

41. Protein secondary structure

42. Protein secondary structure