Unfolding of helical trans-β2,3-hybrid peptides with (α-β)nα composition, when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; C-terminal region of these peptides were first to unwind and the process propagated towards N terminus with more and more β residues equilibrating from the gauche to the anti rotameric state across Cα£Cβ. This is evidenced by clear change in their CβH signal splitting, 3JCαH-CβH values, and sequential disappearance of i,i+2 NOEs. Helix-strand hybrid: Unfolding of helical trans-β2,3-hybrid peptides with (α-β)nα composition when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; the C-terminal region of these peptides were first to unwind and the process propagated towards the N terminus with more and more β residues equilibrating from gauche to anti rotameric states across Cα£Cβ. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.