Residue based control of specific helical folding is explored in hybrid peptide oligomers consisting of alternating L-Ala and cis-b-furanoid sugar amino acid (FSAA) residues as building blocks; two series of these hybrid oligomers are designed, synthesized and extensively characterized by using NMR, CD, FT-IR and MD simulation studies; results show the coexistence of left-handed 11- and 14/15-helical conformations in these short oligomers of Boc-(a/b) and Boc-(b/a) series.
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