Tutorial 4 Practice Questions

LO8 and 9
LO8 - PROTEINS
1. Four structures – find the α carbon!
 1. Choose the correct answer

A. These 4 structures 50% 50%

represent the same

amino acid
B. There are at least
two different amino
acids represented
by these structures

A. B.
4 structures – find the α carbon!
2. These amino acids are considered____ and ____.

25% 25% 25% 25%

A. polar (uncharged); polar
(charged)
B. polar (uncharged); nonpolar
C. nonpolar; polar (uncharged)
D. nonpolar; nonpolar

A. B. C. D.
Phenylalanine Tyrosine

polar group
 3. The only amino acid in which the α amino
group is directly linked to the R group is______.
A. tyrosine 20% 20% 20% 20% 20%

B. proline
C. phenylalanine
D. tryptophan
E. cysteine

A. B. C. D. E.

The α amino group is the amino group directly linked to the α carbon.
Compare the α carbon of glycine to that
of proline (red circles)

α carbon

α amino group

glycine proline
4. A molecular biologist wishes to change an aspartic acid
within a protein to the most similar uncharged amino acid.
She should change it to___________.

25% 25% 25% 25%

A. A
B. B
C. C
D. D

A. B. C. D.
 asparagine isoleucine glutamic acid

aspartic acid
glutamine (drawn in the
non-ionized
state)
 5. A short linear peptide has the following sequence:
VALLAV (Val-Ala-Leu-Leu-Ala-Val). At pH values
between 6 and 7, the peptide will have________
A. a net neutral charge 25% 25% 25% 25%

B. a net positive
charge
C. a net negative
charge
D. no charges

A. B. C. D.
 Domains, modules and motifs

• we will use the word domain

• refers to an area of the protein in which a set of
secondary structures interact to form a fully or
partially self-contained unit
• we would tend to apply “domain” to a protein
that is complex enough that it has at least two
domains, or one domain and an unstructured
region
• could also apply “domain” to a region of distinct
function (e.g. the catalytic domain)
 6. The region marked “α1” is an example of
__________.
A. primary structure 20% 20% 20% 20% 20%

B. secondary structure
C. tertiary structure
D. quaternary
structure
E. a domain

A. B. C. D. E.
7. The region marked “α1+α2+α3 is an example
of __________.
A. primary structure 20% 20% 20% 20% 20%

B. secondary structure
C. tertiary structure
D. quaternary
structure
E. a domain

A. B. C. D. E.
8. The formation of the α1 helix is primarily due
to __________.
A. H bonding between R 25% 25% 25% 25%
groups
B. H bonding between R
groups and atoms in
the peptide backbone
C. H bonding between
groups in the peptide
backbone
D. disulfide bond
formation A. B. C. D.
 9. Uncharged free amino acids are not found
because______.
A. the + and – charges cancel 20% 20% 20% 20% 20%
out
B. free amino acids do not
occur in the cell
C. the pKa values of the
amino and carboxyl
groups are too similar
D. the R group is uncharged
E. the pKa values of the
amino and carboxyl
groups are distinctly
different
A. B. C. D. E.
A peptide bond in this short peptide is indicated
by the __________.
 10. A peptide bond in this short peptide is
indicated by the_________.
A. blue arrow 20% 20% 20% 20% 20%

B. green arrow
C. orange arrow
D. red arrow
E. black arrow

A. B. C. D. E.
LO9 - LIPIDS
 Which of these structures is not a lipid?

C
D
E
 11. Which of these structures is not a lipid?

A. A 20% 20% 20% 20% 20%

B. B
C. C
D. D
E. E

A. B. C. D. E.
only phospholipids
and many
glycolipids are
triglcerides
 Answers

1. A 9. E
2. C 10. B
3. B 11. B
4. A
5. A
6. B
7. E
8. C