Modulating the Structural Properties of α,γ-Hybrid Peptides by α-Amino Acid Residues: Uniform 12-Helix Versus "Mixed" 12/10-Helix.

@article{Misra2017ModulatingTS,
  title={Modulating the Structural Properties of α,γ-Hybrid Peptides by α-Amino Acid Residues: Uniform 12-Helix Versus "Mixed" 12/10-Helix.},
  author={Rajkumar Misra and K. Muruga Poopathi Raja and Hans-J{\"o}rg Hofmann and Hosahudya N Gopi},
  journal={Chemistry},
  year={2017},
  volume={23 65},
  pages={16644-16652}
}
The most important natural α- and 310 -helices are stabilized by unidirectional intramolecular hydrogen bonds along the helical cylinder. In contrast, we report here on 12/10-helical conformations with alternately changing hydrogen-bond directionality in sequences of α,γ-hybrid peptides P1-P5 [P1: Boc-Ala-Aic-Ala-Aic-COOH; P2: Boc-Leu-Aic-Leu-Aic-OEt; P3… CONTINUE READING