AbstractProtein structures are typically made up of well‐defined modules, called secondary structures. A hierarchical model of protein folding may start with the formation of five‐membered non‐covalently‐linked ring motifs involving O⋅⋅⋅C=O and N−H···N interactions connecting two consecutive peptide groups. Some of these interactions lead to polyproline II structure, which are known to occur in the unfolded state of proteins. These interactions constitute different types of γ‐turns, providing the sharpest reversal of the chain direction. Occurring transiently in the unfolded state, and in tandem, they can lead to β‐turns. One of the β‐turns (type I) is predisposed (from a consideration of residue usage) to form the N‐terminal of an α‐helix, which then propagates toward its C‐terminal direction. O⋅⋅⋅C=O interactions encompass four distinct types of conformational features, and one of them has very similar backbone torsion angles as the polyproline II (PPII) conformation and can thus contribute to the formation of PPII helix. An adjustment from these angles can also drive the formation of β‐strand. N−H···N interactions can also constitute capping interaction at helix termini and can link a PPII helix to an α‐helix. Thus, the polypeptide backbone is endowed with all the features that can initiate the formation of secondary structural elements, and the γ‐turn motifs (resulting from O⋅⋅⋅C=O and N−H···N interactions) are the basic units the protein structures are made up of.