Extreme stability of an unsolvated alpha-helix.

@article{Kohtani2004ExtremeSO,
  title={Extreme stability of an unsolvated alpha-helix.},
  author={Motoya Kohtani and Thaddeus C Jones and Jean E Schneider and Martin F Jarrold},
  journal={Journal of the American Chemical Society},
  year={2004},
  volume={126 24},
  pages={7420-1}
}
High-temperature ion mobility measurements have been performed for alpha-helical Ac-A15K+H+ and globular Ac-KA15+H+ peptides. The alpha-helical and globular conformations do not melt into random coils as the temperature is raised. Instead, both conformations survive to the point where the peptide signals vanishes due to fragmentation. This occurs at 600 K for the globular Ac-KA15+H+ peptide and at 725 K for the alpha-helical Ac-A15K+H+. For the helical Ac-A15K+H+ peptide it appears that… CONTINUE READING

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