Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric alpha-helical state into insoluble beta-sheet aggregates.

@article{Szyperski1998PulmonarySP,
  title={Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric alpha-helical state into insoluble beta-sheet aggregates.},
  author={Thomas Szyperski and Guy Vandenbussche and Tore Curstedt and Jean Marie Ruysschaert and Kurt W{\"u}thrich and Jan J Johansson},
  journal={Protein science : a publication of the Protein Society},
  year={1998},
  volume={7 12},
  pages={2533-40}
}
In the 35-residue pulmonary surfactant-associated lipopolypeptide C (SP-C), the stability of the valyl-rich alpha-helix comprising residues 9-34 has been monitored by circular dichroism, nuclear magnetic resonance, and Fourier transform infrared spectroscopy in both a mixed organic solvent and in phospholipid micelles. The alpha-helical form of SP-C observed in freshly prepared solutions in a mixed solvent of CHCl3/CH3OH/0.1 M HCl 32:64:5 (v/v/v) at 10 degrees C undergoes within a few days an… CONTINUE READING

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