Defining the secondary and tertiary structure of the protein

Question

1. The primary structure of a protein is important for defining the secondary and tertiary structure of the protein.

• True
• False

2. An alpha helix:

• Is an example of a super primary structure?
• Is disrupted by the amino acid glycine
• Can be combined with other alpha helices to form super secondary structures
• Occurs by hydrogen bonding that is perpendicular to the helix axis
• All of the above

3. Beta pleated sheets can exist with their peptide chains either in parallel or anti-parallel orientations.

• True
• False

4. Allosteric regulation of myoglobin function refers to positive cooperatively of oxygen binding to this protein.

• True
• False

5. The difference between fetal and adult hemoglobin with regard to oxygen binding is due to:

• Adult hemoglobin has two gamma chains whereas the fetal hemoglobin has two beta chains
• Fetal hemoglobin has an amino acid substitution in one of its chains that result in a histamine being replaced by a serine.
• Fetal hemoglobin has more positive charges for binding BPG.
• Fetal hemoglobin binds more tightly to 2, 3 bisphosphoglycerate
• None of the above