Short alanine-based peptides may form 3(10)-helices and not alpha-helices in aqueous solution.

@article{Miick1992ShortAP,
  title={Short alanine-based peptides may form 3(10)-helices and not alpha-helices in aqueous solution.},
  author={Siobhan M. Miick and G. Vilar Martinez and Wayne R. Fiori and Averett Todd and Glenn L. Millhauser},
  journal={Nature},
  year={1992},
  volume={359 6396},
  pages={
          653-5
        }
}
Short alanine peptides, containing 16 or 17 residues, appear to form alpha-helices in aqueous solution. But the main spectroscopic analyses used on helical peptides (circular dichroism and nuclear magnetic resonance) cannot distinguish between an alpha-helix (in which the ith residue is hydrogen-bonded to residue i + 4; ref. 9) and the next most common peptide helix, the 3(10)-helix10 (i-->i + 3 hydrogen-bonding). To address this problem we have designed single and doubly spin-labelled… CONTINUE READING

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