Practice Questions
1. Explain why glycine is considered unique among the standard amino acids.
2. Describe the general structure of an α-amino acid and label the chiral center
3. Differentiate between aliphatic, aromatic, acidic, basic, and sulfur-containing amino
acids with one example each.
4. Name the amino acid side chains commonly modified by:
Phosphorylation, N-linked glycosylation, O-linked glycosylation, Acetylation,
Ubiquitination
5. How can a single type of PTM (e.g., phosphorylation) have different functional
outcomes depending on the site and context?
6. Name the two most common regular secondary structures and their key stabilizing
interactions.
7. State the hydrogen bonding pattern in an α-helix (which atoms and how many
residues apart)
8. Differentiate between parallel and antiparallel β-pleated sheets.
9. Explain why glycine and proline are considered “helix breakers”.
10. Describe the chemical reaction involved in peptide bond formation between two
amino acids.
11. Define φ (phi) and ψ (psi) dihedral angles in a polypeptide chain and explain their
relation to peptide bond planarity
12. How is the Ramachandran plot used in protein structure validation, and what does
an outlier indicate?