A left-handed 3(1) helical conformation in the Alzheimer Abeta(12-28) peptide.

@article{Jarvet2003AL3,
  title={A left-handed 3(1) helical conformation in the Alzheimer Abeta(12-28) peptide.},
  author={J{\"u}ri Jarvet and Peter Damberg and Jens Danielsson and Ingela Johansson and Lars E Eriksson and Astrid Gr{\"a}slund},
  journal={FEBS letters},
  year={2003},
  volume={555 2},
  pages={
          371-4
        }
}
We show for the first time that the secondary structure of the Alzheimer beta-peptide is in a temperature-dependent equilibrium between an extended left-handed 3(1) helix and a flexible random coil conformation. Circular dichroism spectra, recorded at 0.03 mM peptide concentration, show that the equilibrium is shifted towards increasing left-handed 3(1) helix structure towards lower temperatures. High resolution nuclear magnetic resonance (NMR) spectroscopy has been used to study the Alzheimer… CONTINUE READING

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