Chapter 8: Three-Dimensional Structures of Proteins

Matching
A)

tertiary structure

B)

keratin

C)

molecular chaperone

D)

hydropathy value

E)

cis

F)

trans

G)

forbidden conformation

H)

regular secondary structure

I)

collagen

J)

peptide group

K)

ribonuclease A

L)

alpha

1. The helix and the pleated sheet, with their repeating and values, are examples of
______.
Ans: H
Level of Difficulty: Easy
Section 8-1. Secondary Structure
2. ______ is found in bone, teeth, cartilage, and tendons.
Ans: I
Level of Difficulty: Easy
Section 8-1. Secondary Structure

3. The arrangement of the regular structural elements and the positions of atoms in the protein
are considered part of ______.
Ans: A
Level of Difficulty: Easy
Section 8-3. Globular Proteins

4. A historical denaturation/renaturation experiment was carried out using the protein ______.
Ans: K
Level of Difficulty: Easy
Section 8-4. Protein Stability

5. A rigid, planar structure consisting of about 40% double bond character is characteristic of a
______.
Ans: J
Level of Difficulty: Easy
Section 8-1. Secondary Structure

6. A good way to predict whether an amino acid side chain is on the outside or inside of a
protein is to use its ______.
Ans: D
Level of Difficulty: Easy
Section 8-4. Protein Stability

7. A protein found in hair, horn, nails, and feathers is ______.

Ans: B
Level of Difficulty: Easy
Section 8-1. Secondary Structure

8. In most peptide groups (with the exception of proline) the ______ conformation is not
commonly observed
Ans: E
Level of Difficulty: Easy

Section 8-1. Secondary Structure

9. In a ______, the and angles bring groups closer than their van der Waals distances.
Ans: G
Level of Difficulty: Easy
Section 8-1. Secondary Structure

Multiple Choice
10. In a Ramachandran diagram, ______ of the area represents allowed conformations of a
polypeptide chain.
A) more than 90%
B) more than 50%
C) about 50%
D) less than 25%
E) none of the above
Ans: D
Level of Difficulty: Medium
Section 8-1. Secondary Structure

11. In a protein, the most conformationally restricted amino acid is ______; the least
conformationally restricted is ______.
A) Trp, Gly
B) Met, Cys
C) Pro, Gly
D) Ile, Ala
E) Ala, Pro
Ans: C
Level of Difficulty: Easy

Section 8-1. Secondary Structure

12. Conformation(s) that has (have) both a favorable hydrogen bonding pattern and and
values that fall within the allowed Ramachandran conformational regions is (are) _.
A) helix
B) collagen helix
C) sheet
D) All of the above
E) None of the above
Ans: D
Level of Difficulty: Easy
Section 8-1. Secondary Structure

13. Which one of these characteristics is not true for the helix?
A) There are 3.6 amino acids per turn.
B) There is a requirement for glycine every third amino acid residue.
C) A hydrogen bond forms between the carbonyl oxygen of the nth amino acid residue and the
-NH group of the (n + 4)th amino acid residue.
D) Proline is typically not found in the helix.
E) It is right-handed.
Ans: B
Level of Difficulty: Easy
Section 8-1. Secondary Structure

14. Which of these characteristics does not describe the sheet?

A) Side chains are located both above and below the sheet.
B) sheets usually exhibit right-handed twists.

C) There are two forms, parallel and antiparallel.

D) The sheets contain as few as two and as many as 22 polypeptide chains.
E) Parallel sheets containing fewer than five chains are the most common.
Ans: E
Level of Difficulty: Medium
Section 8-1. Secondary Structure

15. Which statement below does not describe fibrous proteins?

A) Domains are compact and globular.
B) These proteins are usually dominated by a single type of secondary structure.
C) These proteins usually perform a protective, connective, or supportive role in the organism.
D) Domains are usually stiff and elongated.
E) The proteins are usually water soluble.
Ans: A
Level of Difficulty: Easy
Section 8-2. Fibrous Proteins

16. Which of the following statements about keratin is false?

A) Its primary structure consists of a 7-residue repeat, with nonpolar residues predominating at
the first and fourth residues.
B) The classification of keratin as hard or soft is determined by the proportion of proline
residues.
C) It consists of coiled-coil structures, which form dimers and then associate to form
protofilaments.
D) The coiled-coil structures account for the springiness of hair and wool fibers.
E) Individual chains are cross-linked by disulfide bonds.
Ans: B
Level of Difficulty: Medium
Section 8-1. Secondary Structure

17. Which of the following statements does not apply to collagen?

A) It contains hydroxylated amino acids.
B) The polypeptide forms a left-handed helix.
C) Hydrogen bonds between the -OH groups of Hyp residues stabilize the helix.
D) There is an absolute requirement for glycine every third position.
E) The triple helical structure twists in the right-handed direction.
Ans: C
Level of Difficulty: Medium
Section 8-1. Secondary Structure

18. What kind(s) of structures would be described as nonrepetitive protein structures?

A) Random coils, which are totally disordered.
B) Denatured proteins, which are fully unfolded and have rapidly fluctuating conformations.
C) A bulge, which forms when an extra residue occurs in a sheet and is not hydrogenbonded to a neighboring strand.
D) All of the above statements describe nonrepetitive protein structures.
E) None of the above.
Ans: C
Level of Difficulty: Medium
Section 8-1. Secondary Structure

19. Crystalline proteins assume nearly the same structures as the proteins in solution. Several
lines of evidence support this statement; which is the most compelling?
A) A crystalline protein is essentially in solution, because of the waters of hydration that
crystallize along with the protein.
B) Electron density maps can be obtained at high resolution.
C) Different crystal forms of the same protein have virtually identical conformations.

D) Enzymes are often catalytically active in solution.

E) Enzymes are often catalytically active in the crystalline state.
Ans: E
Level of Difficulty: Medium
Section 8-3. Globular Proteins

20. In the absence of ascorbic acid, prolyl oxidase is unable to oxidize proline residues in
collagen to hydroxyproline, resulting in:
A) sickle-cell anemia
B) prion diseases
C) amyloid formation
D) the disease scurvy
E) brittle hair and nails
Ans: D
Level of Difficulty: Easy
Section 8-2. Fibrous Proteins

21. Of the following, which amino acid is least likely to be found on the surface of a singlesubunit protein?
A) Gly
B) Asp
C) Lys
D) Trp
E) Ser
Ans: D
Level of Difficulty: Easy
Section 8-3. Globular Proteins

22. Lysine can form a salt bridge by associating with a nearby _____ residue.

A) Gly
B) Ser
C) Glu
D) Gln
E) Pro
Ans: C
Level of Difficulty: Easy
Section 8-4. Protein Stability

23. The low pH found in the gut can enhance the digestibility of dietary protein by causing
_____.
A) Amide hydrolysis
B) Protein denaturation
C) Disulfide reduction
D) Prion formation
E) Cysteine oxidation
Ans: B
Level of Difficulty: Easy
Section 8-4. Protein Stability
24. The most conformationally-restricted amino acid is _________.
A) proline
B) alanine
C) tryptophan
D) glycine
E) tyrosine
Ans: A
Level of Difficulty: Easy
Section 8-1. Secondary Structure

25. For -sheets, the terms parallel and anti-parallel refer to ___________.
A) the direction of the associated peptide strands
B) the orientation of the amide crosslinks
C) the quaternary structure of the protein
D) the orientation of the hydrogen bonding
D) the topology of the reverse turns
Ans: A
Level of Difficulty: Easy
Section 8-1. Secondary Structure

26. _________ is a triple-helical fibrous protein.

A) -Keratin
B) -Keratin
C) Collagen
D) RNase A
E) None of the above
Ans: C
Level of Difficulty: Easy
Section 8-1. Secondary Structure
27. In protein X-ray crystallography, X-ray radiation is utilized because _______.
A) X-ray lenses are very precise
B) the colors of protein crystals block visible light
C) X-rays are effectively diffracted by the atomic nuclei
D) X-ray diffraction patterns are most readily interpreted
E) the wavelength of X-ray radiation is close to the observed covalent bond lengths.
Ans: E
Level of Difficulty: Medium
Section 8-3. Globular Proteins
28. Secondary structural elements are often observed in groupings commonly called________.
A) motifs
B) domains
C) clusters
D) lobes

E) rolls
Ans: A
Level of Difficulty: Easy
Section 8-3. Globular Proteins
29. Which of the following is not an example of a supersecondary structural element?
A) -helix
B) -barrel
C) immunoglobin fold
D) -hairpin
E) Greek key motif
Ans: A
Level of Difficulty: Medium
Section 8-3. Globular Proteins
30. The Protein Data Bank (PDB) is a database that primarily contains information about
_____.
A) gene sequences
B) biohazards
C) enzyme specificity
D) protein structure
E) protein function
Ans. D
Level of Difficulty: Easy
Section 8-3. Globular Proteins
31. Non-covalent forces that stabilize protein structure include all of the following except
__________.
A) the hydrophobic effect
B) salt bridges
C) metal-ion coordination
D) hydrogen bonding
E) disulfide bridges
Ans: E
Level of Difficulty: Easy
Section 8-4. Protein Stability
32. The classic experiment demonstrating that reduced and denatured RNase A could refold into
the native form demonstrates that _______.
A) 1 structure can determine 3 structure

B)
C)
D)
E)

denaturation does not disrupt protein 2 structure

disulfide bonds do not stabilize folded proteins
proteins are extraordinarly stable
none of the above

Ans: A
Level of Difficulty: Easy
Section 8-4. Protein Stability

33. The reaction of carbonic anhydrase catalyzes:

A) the formation of carbamates with the concomitant release of protons
B) the hydration of bicarbonate, resulting in the formation of carbonic acid
C) the reduction of carbon dioxide with the concomitant consumption of protons
D) the hydration of carbon dioxide, forming bicarbonate and protons
E) the hydrolysis of carbamates with the concomitant consumption of protons
Ans: D
Level of Difficulty: Easy
Section: 8-3. Globular Proteins