Arrange the three residues, glycine, phenylalanine and proline, in the decreasing order of backbone flexibility
(1) Gly > Phe > Pro
(2) Pro > Gly > Phe
(3) Phe > Pro > Gly
(4) It is not possible to comment
Backbone flexibility in amino acids depends on the torsional freedom of the main chain (Φ, Ψ angles).
Analyzing each residue:
-
Glycine (Gly)
- Most flexible due to the absence of a bulky side chain (R = H).
- Can adopt a wide range of Φ and Ψ angles.
- Appears frequently in turns and flexible regions.
-
Phenylalanine (Phe)
- Has a bulky benzyl side chain but does not significantly restrict backbone flexibility.
- Still relatively flexible compared to rigid residues like Proline.
-
Proline (Pro)
- Least flexible because its side chain forms a ring with the backbone, restricting the Φ angle (~ -60°).
- Has limited conformational freedom, often found in turns and cis-peptide bonds.
Arranging in decreasing order of flexibility:
Glycine > Phenylalanine > Proline
Thus, the correct answer is:
(1) Gly > Phe > Pro