Chapter 3

Amino Acids, Peptides and Proteins

1. At very low pH most amino acids is have a _____ charge.

Ans: positive

Link to: 3.1

Difficulty: Easy

2. Disulfide bonds are formed between two ______amino acids.

Ans: cysteine

Link to: 3.1

Difficulty: Easy

3. In the condensation of two amino acids one molecule of ______is lost.

Ans: water

Link to: 3.2

Difficulty: Easy

4. Amino acids linked together in a chain are called a ______.

Ans: polypeptide

Link to: 3.2

Difficulty: Easy

5. Protein in the food we eat is digested by enzymes called ______.

Ans: peptidases

Link to: 3.2

Difficulty: Easy

6. A deficiency in vitamin C causes defects in collagen, which is classified as a _____ protein.

Ans: structural

Link to: 3.3

Difficulty: Easy

7. The protein ______participates in oxygen dispersal in muscle.

Ans: myoglobin

Link to: 3.3

Difficulty: Easy

8. A polypeptide can fold into an individual unit of structure called a ______.

Ans: domain

Link to: 3.3

Difficulty: Easy

9. A protein that contains more than one subunit is called ______.

Ans: oligomeric

Link to: 3.4

Difficulty: Easy

10. A secondary structure which forms a coiled shape with a specific repeating pattern, stabilized by hydrogen bonds, is called a(n)______.

Ans: alpha helix

Link to: 3.4

Difficulty: Medium

11. The sequence of amino acids in a protein, from N to C-terminus, is referred to as the ______structure.

Ans: primary

Link to: 3.4

Difficulty: Easy

12. Related proteins contain large regions of sequence ______.

Ans: homology

Link to: 3.5

Difficulty: Easy

13. The purity and size of a protein can be determined by ______.

Ans: electrophoresis

Link to: 3.5

Difficulty: easy

14. The amino acid which gives the taste of unami is ______.

Ans: glutamic acid

Link to: 3.5

Difficulty: Easy

15. Sickle cell anemia is caused by an amino acid ______.

Ans: substitution (or replacement)

Link to: 3.5

Difficulty: easy

16. The collective group of all the proteins is called the:

a) protosome.

b) proteome.

c) genome.

d) prion.

e) liposome.

Ans: b

Link to: Intro

Difficulty: Easy

17. Amino acids are considered zwitterions because they:

a) exist as dipolar ionic species.

b) were discovered by H. Zwitter.

c) are white solids.

d) are soluble in water.

e) conduct an electric current.

Ans: a

Link to: 3.1

Difficulty: Easy

18. The pK values for amino groups are typically in the pH range:

a) 0-2

b) 4-6

c) 6-8

d) 8-10

e) 4-8

Ans: d

Link to: 3.1

Difficulty: Medium

19. Amino acids contain the following groups linked to a carbon:

a) an amino group and a carboxylate group.

b) an amino group and an R group .

c) a carboxylate group and an R group.

d) an amino group and a carboxylate group and an R group.

e) none of the above

Ans: d

Link to: 3.1

Difficulty: Medium

20. The amino acids with charged side chains include:

a) aspartate, glutamate, lysine and arginine.

b) aspartate, glutamate and glycine.

c) aspartate, lysine and arginine.

d) aspartate, glutamate, lysine, glycine and arginine.

e) none of the above

Ans: a

Link to: 3.1

Difficulty: Medium

21. The net charge of the peptide Arg-Phe-Gly-Lys-Glu at pH 7 is:

a) +2

b) +3

c) -2

d) +1

e) -3

Ans: d

Link to: 3.1

Difficulty: Medium

22. Which of the following is not an amino acid inserted into proteins by a “dedicated” tRNA?

a) selenocysteine

b) proline

c) phosphoserine

d) glycine

e) asparagine

Ans: c

Link to: 3.1

Difficulty: Medium

23. In order to design a drug that could enter a cell, a scientist might consider how it would interact with a ____ protein located on the cellular membrane.

a) defense

b) structural

c) catalytic

d) immune

e) transport

Ans: e

Link to: 3.3

Difficulty: Medium

24. Which of the following characteristics is consistent with the description of a fibrous protein, but not a globular protein?

a) water insoluble

b) dissolved in biological fluids

c) high content of polar amino acids

d) low tensile strength

e) often function as transport proteins

Ans: a

Link to: 3.4

Difficulty: Medium

25. The heme found in myoglobin is a:

a) domain.

b) prosthetic group.

c) zinc finger.

d) peptide.

e) none of the above

Ans: b

Link to: 3.4

Difficulty: Medium

26. Which of the following is not a type of secondary structure found in proteins?

a)  sheet

b)  helix

c) random coil

d) random turn

e) disulfide bond

Ans: e

Link to: 3.4-3.5

Difficulty: easy

27. If designing a drug that inhibited a large, multisubunit enzyme, it would be important to know how the drug interacted with the:

a) primary structure.

b) mRNA structure.

c) secondary structure.

d) tertiary structure.

e) quaternary structure.

Ans: e

Link to: 3.4

Difficulty: Medium

28. Proteins with charges can be separated by ______chromatography.

a) exclusion

b) size

c) affinity

d) ion exchange

e) gel

Ans: d

Link to 3.5:

Difficulty: Medium

29. Protein sequences can be determined by:

a) amino acid sequencing of the protein.

b) determining the amino acid composition.

c) sequencing the DNA of the protein’s corresponding gene.

d) a and b

e) a and c

Ans: e

Link to: 3.5

Difficulty: Medium

30. Protein sequence data cannot be used to:

a) determine mutations.

b) estimate three-dimensional structure.

c) determine the exact DNA sequence.

d) deduce about biological function.

e) obtain evolutionary data.

Ans: c

Link to: 3.5

Difficulty: Medium

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