Can Helical Peptides Unwind One Turn at a Time? ‐ Controlled Conformational Transitions in α,β 2,3 ‐Hybrid Peptides

Unfolding of helical trans ‐β 2,3 ‐hybrid peptides with (α–β) n α 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 C α C β . This is evidenced by clear change in their C β H signal splitting, 3 J CαH–CβH values, and sequential disappearance of i , i +2 NOEs.