FIBROUS and GLOBULAR PROTEINS

1. Which statement below does not describe fibrous proteins?

A)
B)
C)
D)
E)

Domains have a globular fold.

These proteins usually contain only one type of secondary structure.
These proteins usually exhibit structural or protective characteristics.
These proteins have usually elongated hydrophilic surfaces.
These proteins are usually insoluble in water.

Ans: A

2. Of the following, which amino acid is most likely to be found in position 1 or 4 on

keratin?
A) Phe
B) Ala
C) Lys
D) Trp
E) Pro

Ans: B

3. Based on what you know about fibrous protein structure and sequence, what type of
fibrous protein is this sequence most likely to from (You can assume that the protein
is longer than what is shown and is repeating as shown, also note the polarity of each
amino acid.)?

Val Cys Lys Val - Cys Ala Cys - Val Cys Lys Val - Cys Ala Cys

A)
B)
C)
D)

a keratin
keratin
collagen
This sequence cannot be from any of the structural proteins.

Ans: A

4. When considering fibrous proteins, which of the following statements is TRUE?

A)
B)
C)
D)

Non covalent interactions contribute to the strength of all of these proteins.

All of them consist of a helix structure.
Decrease in amounts of any of them cause scurvy.
All of these are true of fibrous proteins.
Ans: A

5. A fibrous protein has the following repeated unit: G-S-G-A-G-A.

which kind of protein is it?
a) Collagen
b) Silk fibroin
c) a-keratin

Asn: B

6. Woolen clothes shrink if they are washed in hot water and dried in hot, while silk ones
dont. Can you explain why?

Asn:
wool is characterized by extensive polypeptide chains which are converted into shorter ahelices by hot, instead b-sheet of silk proteins are more stable than wool due to their
small and close side chains

7.
A)
B)
C)
D)

Myoglobins primary physiological role is to facilitate oxygen ________.

discard
metabolism
reduction
diffusion

Ans: D

8. Myoglobin and a single chain of hemoglobin have similar ______ structures.

A) primary
B) secondary
C) tertiary
D) quaternary
E) none of the above
Ans: C

9.
A)
B)
C)
D)
E)

Hemoglobin's p50 value is about ______ as great as myoglobin's p50 value.

one-tenth
half
twice
ten times
twenty times
Ans: D

10. While the binding of O2 to myoglobin as a function of pO2 is described by a simple

__________ curve, the binding to hemoglobin is described by a more complex ______
curve.
A) sigmoidal; hyperbolic
B) hyperbolic; sigmoidal
C) exponential; hyperbolic
D) sigmoidal; bell-shaped
E) hyperbolic; concave
Ans: B

11. The Bohr effect refers to

A) the decrease in affinity of Hb for O2 when the pH goes down
B) the decrease in affinity of Hb for O2 when the pH goes up
C) the increase in the affinity of Hb for O2 when the O2 concentration goes up
D) the decrease in affinity of Hb for O2 when the BPG concentration goes up
E) the decrease in affinity of Hb for O2 when the BPG concentration goes down

Ans: A

12. The rearrangement of T state hemoglobin to the R state

A) occurs in each protein subunit independently when its heme binds oxygen.
B) requires the binding of at least three oxygen molecules.
C) increases the ion pairing interactions of the C-terminal amino acids.
D) involves the movement of the Fe(II) into the heme plane.
E) opens a central cavity for BPG binding.
Ans: D
13. BPG stands for
A) biphenylglycine.
B) boronylphenylglutamate.
C) Bisphosphoglyceric acid.
D) bisphenylglycerol.
E) betapropylglutamine.

Ans: C

14. Muscle contraction is directly caused by

A) structural changes in actin.
B) structural changes in myosin.
C) thick and thin filaments sliding past each other.
D) structural changes in the Z disk.
E) None of the above is correct.

Ans: C

15. During muscle contraction

A) myosin pulls actin filaments toward the M disk.
B) myosin pushes actin filaments toward the Z disk.
C) actin pulls myosin toward the Z disk.
D) actin pushes myosin toward the M disk.
E) All of the answers above are correct.

Ans: A

16. Muscle contraction is triggered

A) in response to an increase in the cytoplasmic Ca2+ concentration.
B) in response to a decrease in the cytoplasmic Ca2+ concentration.
C) in response to an increase in the cytoplasmic cAMP concentration.
D) in response to a decrease in the cytoplasmic cAMP concentration.
E) in response to an increase in the cytoplasmic titin concentration.

Ans: A

17. IgG is one of five classes of antibodies that can be produced by our immune system.
IgGs have a molecular mass of approximately 150 kDa, what is their subunit composition?
A) 2 light chains and 2 heavy chains
B) 2 light chains, 2 heavy chains, and a J chain
C) 4 light chains, 4 heavy chains, and a J chain
D) 6 light chains, 6 heavy chains, and a J chain
E) 10 light chains, 10 heavy chains , and a J chain.
Ans: A

18. Humoral immunity refers to that part of the immune response that is mediated by
A) T lymphocytes.
B) antibodies.
C) antigens.
D) the thymus.
E) the skin.
Ans: B

19. Which statement about antigen-binding sites in antibodies is false?

A) An antigen-binding site on an IgG is formed by the variable region of a light chain and
the variable region of a heavy chain.
B) The antigen-binding site is composed of two Ig folds.
C) Antigen-binding specificity is determined by the sequences of the hypervariable
sequences in both the light chain and the heavy chain.
D) Antigen binding specificity is determined exclusively by the sequences in the carboxyterminal in the heavy chain.
Ans: D

20. The graph below shows the O2-binding curves for myoglobin (Mb) and hemoglobin (Hb).
a. Label the two curves (indicate which one represents Mb and which one represents Hb).
b. What is the difference between myoglobin and hemoglobin that cause the O2-binding
curves to so be different?
c. Why is it important that hemoglobin has these particular O2-binding characteristics?

Asn:
a. See the graph
b. b. Mb has one subunit, Hb has 4 subunits. The sigmoid binding curve is a consequence of
positive cooperativity between the 4 O2-binding sites in Hb. The hyperbolic binding curve
for myoglobin is the result of oxygen binding reaction being noncooperative.
c. As a consequence of positive cooperation Hb has a high affinity for O2 when the O2
concentration is high (in the lungs) and low affinity for O2 when the O2 concentration is low (in
the tissues). As a consequence Hb binds large amount of O2 in the lungs and releases large
amounts of O2 in the tissues, resulting in efficient transport of O2.