Question

1. Which non-covalent interaction is primarily
responsible for stabilizing a helices, ß sheets, and ß
turns?
a. Hydrophobic interactions.
b. Ion-pairing.
c. Hydrogen bonding.
d. Stacking of aromatic rings.
e. Van der Waals interactions.

2.Which is not associated with the formation of oligomers?
a. Increased stability compared to the dissociated subunits.
b. The formation of active sites between adjacent subunits.
c. Contact between the subunits that allows for changes in
quaternary structure when ligands bind. This can control
biological activity.
d. Increased efficiency by synthesizing smaller subunits
rather than a single chain the same size as the oligomer.
e. An enhanced ability to adopt F and ? angles outside the
common ranges.

3. Would you expect myoglobin that is injected
intravenously to perform the same function as
hemoglobin? Explain.
a. No, myoglobin cannot release oxygen as well to the
tissues.
b. No, because the heme of myoglobin binds oxygen at a
different coordination site.
c. No, because 2,3-BPG completely inhibits the binding of
oxygen to myoglobin.
d. Yes, in the blood myoglobin adopts a similar quaternary
structure as hemoglobin and binds oxygen with positive
cooperativity.
e. Yes, because both bind oxygen very easily in the lungs.