The ability of α,β2,3-hybrid peptides with a heterochiral backbone to exist in a helical, extended, or partially folded state depending on the solvation conditions employed was investigated. The preference was found to be directly dictated by Cα-Cβ torsions in the β-residues. α,β-Hybrid peptides with a heterochiral backbone show the ability to exist in a helical, extended, or partially folded conformation depending on the solvation conditions employed. Copyright © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.