 Solution

View the backbone along N–C${}_{\alpha }$ to display $\varphi =\angle (C_{i-1}^{\prime },N_i,C_{\alpha i},C_i^{\prime })$ in a Newman projection. The front amide nitrogen carries the preceding carbonyl and H, while the back C${}_{\alpha }$ carries the next carbonyl, H and side chain. Rotation changes the contacts among these groups. A corresponding view along C${}_{\alpha }$–C${}^{\prime }$ displays $\psi$. The peptide C${}^{\prime }$–N bond itself is approximately planar and is not the freely rotating bond in either definition.

glycine replaces the side chain by a second hydrogen. Removing C${}_{\beta }$ removes many contacts that exclude backbone arrangements for other residues, so its allowed $\varphi ,\psi$ region is much broader and includes substantial positive-$\varphi$ space. Its alpha carbon is also achiral, so the steric map is approximately mirror-symmetric between positive and negative torsions in the simple isolated-residue model.

proline closes a five-membered ring from C${}_{\alpha }$ through three methylenes back to nitrogen. In the N–C${}_{\alpha }$ projection, the nitrogen's side-chain arm and C${}_{\alpha }$'s C${}_{\beta }$ arm are tied together, preventing unrestricted relative rotation. Its $\varphi$ is consequently confined near the usual negative-$60^{\circ }$ region rather than exploring the broad range of an acyclic amino acid. proline also lacks a backbone N–H donor when incorporated into an ordinary internal peptide. Ring closure restricts $\varphi$ strongly, but does not freeze every backbone or ring degree of freedom. These differences are naturally represented by distinct Ramachandran plots; the original torsion/steric analysis established the basis for such comparisons.^[ref]