Which of the following is an example of tertiary structure
in a protein? polyalanine. a multimeric protein. an a-helix. a b-pleated
sheet. a globular domain.
2. An "oil drop with a polar coat" is a metaphor referring to the three
dimensional structure of: fibrous proteins. collagen. globular proteins.
silk protein. The first and the second choice are both correct.
3. The portion of proteins having the highest mobility are a-helices. bsheets. peptide bonds. surface side chains. aliphatic groups.
4. Which of the following is most correct: Charged amino acids are never
buried in the interior of a protein. Charged amino acids are seldom buried in
the interior of a protein. All hydrophobic amino acids are buried when a
protein folds. Tyrosine is only found in the interior of proteins. Glycine is
rarely found in proteins because it is too destabilizing.
5. Disulfide bonds most often stabilize the native structure of: extracellular
proteins. dimeric proteins. hydrophobic proteins. intracellular proteins.
multisubunit proteins.
6. Buried hydrophobic sidechains in a globular protein fit into a "hole" formed
by the sidechains of 1-3 other amino acids. precisely six other amino acids.
5-7 other amino acids. 9-12 other amino acids. 13-15 other amino acids.
7. The fact that the core of most globular proteins is composed of non-polar
residues is because of van der Waals interactions. hydrogen bonds. a
favorable increase in conformational entropy. the hydrophobic effect.
favorable electrostatic interactions.
8. The fact that the core of most globular proteins is tightly packed is due to
the hydrophobic effect. hydrogen bonding. electrostatic effects. van der
Waals forces. configurational entropy.
9. A hydrogen bond to water that is broken during folding and not reformed
has no effect on the stability of the folded state. decreases the stability of the
folded state by 2 kJ/mol. decreases the stability of the unfolded state by 2
kJ/mol. decreases the stability of the folded state by 20 kJ/mol. decreases
the stability of the unfolded state by 20 kJ/mol.