AbstractThe diverse helices from α‐peptide sequences containing alternating L–Leu and Aib residues are described. The X‐ray crystallography shed some light on the folding pattern of the synthetic peptides. The peptides that contain four and five amino acid residues fold into right‐handed (P) 310‐helical structures. The pentapeptide with ‐Aib‐L–Leu‐OMe C‐terminal segment also forms an open Schellman loop with both i+3→i and weak i+5→i hydrogen bonding interactions in crystal. But the hexapeptide with ‐L–Leu‐Aib‐OMe C‐terminal segment exhibits a right‐handed (P) 310‐helical structure. Surprisingly, the heptapeptide is a hybrid helix comprising of all i+3→i, i+4→i and i+5→i hydrogen‐bonded structure in solid state. The presence of Aib(6) residue at C‐terminus as the penultimate residue might be beneficial in inducing the screw‐sense reversal that gives rise to the helix terminating Schellman motif. The approach and findings presented here will be helpful for foldamer engineering.