In an aqueous environment, very hydrophobic residues such as phenylalanine are typically found:

A. In the interior of a globular protein.

B. On the surface of a globular protein.

C. Phenylalanine actually has a hydrophilic side chain.

Change in pH can alter the charge status of protein molecules in aqueous solution. For example, as pH increases, protein molecules in aqueous solution tend to become 

A. More protonated and more positively charged

B. Less protonated and more negatively charged 

C. More stable and active

Which of the following amino acids has no chiral carbon?

A. Glycine

B. Alanine

C. Proline

D. Serine

Which of the following are basic amino acids and carry positive charges at physiological pH?

A. Valine and Leucine

B. Glutamate and Aspartate

C. Cysteine and Methionine

D. Lysine and Arginine

Which of the following amino acids have
two chiral carbons? 

Calculate pI (isoelectric point) of the following amino acid.  The pKa values of a-carboxyl group, a-amino group, and e-amino group (i.e., side chain) are 2.2, 9.1, and 10.5, respectively. 

What would you expect about the formation of an a-helix for a segment of a protein chain that contains lysine approximately every fourth residue with all other residues being mostly hydrophobic?

A) Helix formation would be favored at neutral pH.

B) Helix formation would be favored at low pH.

C) Helix formation would be favored at high pH.

D) Helix formation would never occur regardless of pH.

C) Helix formation would be favored at high pH.