1.

At the center of all 20 standard amino acids is what is termed the -carbon that is covalently
bonded with four other chemical groups. Which of these four chemical groups is not a normal
component of all amino acids?
A. an amino group
B. a carboxyl group
C. a side chain (R group)
D. a methyl group
2. The isoelectric point, or pI, of an amino acid or a protein is
A. the pH at which the amino acid or protein has no net charge.
B. zero at pH 7.0.
C. the pH at which the amino acid or protein is neither hydrophobic nor hydrophilic.
D. the measure of how hydrophobic an amino acid or protein is.
3. Peptide bonds, which covalently link two amino acids, result from
A. the oxidation of amino acids.
B. the condensation of amino acids.
C. the hydrolysis of amino acids.
D. hydrogen bonds between amino acids
4. Which group or groups on a protein contribute most to its overall acid-base properties?
A. The -amino groups of all nonterminal amino acids.
B. The N-terminal -amino group on the protein.
C. The R groups on the protein.
D. The C-terminal -carboxyl group on the protein.
5. Which of the following is true about the Edman degradation system of sequencing
polypeptides?
A. The Edman degradation system will work on any size polypeptide.
B. In the Edman degradation system the amino-terminal residue is labeled and the polypeptide
is hydrolyzed to its constituent amino acids.
C. In the Edman degradation system the amino-terminal residue is labeled, cleaved and
identified in each successive cycle.
D. The Edman degradation system is carried out on a machine called an edmanator.
6. Enzymes are biological catalysts that enhance the rate of a reaction by:
A. increasing the amount of free energy released
B. decreasing the amount of free energy released
C. increasing the energy of the transition state
D. decreasing the activation energy
7. The three-dimensional structure of macromolecules is maintained primarily through non-
covalent interactions. Which of the following are not considered non-covalent interactions?
A. hydrogen bonds
B. van der Waals interactions
C. amide bonds
D. ionic interactions
8. All of the amino acids that are found in proteins (except proline) contain a(n):
A. carbonyl group
B. carboxyl group
C. ester group
D. amino group
9. Of the 20 standard amino acids, only ______ is not optically active. The reason is that its side
chain _________.
A. alanine; is a simple methyl group
B. glycine; is unbranched
C. lysine; contains only nitrogen.
D. glycine; is a hydrogen atom
10. The side chains of nonpolar amino acids are best categorized as:
A. hydrophobic
B. positively charged
C. negatively charged
D. hydrophilic
11. Trypsin cuts primarily after what type of residue?
A. aliphatic non polar
B. negatively charged
C. small uncharged
D. positively charged
12. Which of the following may prevent Edman sequencing?
A. C-terminal amidation
B. phosphorylation
C. blocked N terminal
D. N-linked glycosylation
Problem Solving
1. Identify the unknown hexapeptide from the following data:
o complete hydrolysis gives equimolar amounts of Arg, Glu, Lys, Phe, Pro, Tyr
o Edman degradation of the hexapeptide gives labeled Phe
o chymotrypsin cleavage gives a tetrapeptide, Phe, and Glu
o Edman degradation of the tetrapeptide gives labeled Lys
o trypsin cleavage gives three dipeptides
o Edman degradation of the dipeptides gives labeled Phe, Pro, and Tyr





Key
1. D
2. A
3. B
4. C
5. C
6. D
7. C
8. D
9. D
10. A
11. D
12. C

Problem Solving
PheLysProArgTyrGlu