Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans.

@article{Killian1996InductionON,
  title={Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans.},
  author={J. Antoinette Killian and I Salemink and Maurits R R de Planque and G{\"o}ran Lindblom and Roger E Koeppe and Denise V Greathouse},
  journal={Biochemistry},
  year={1996},
  volume={35 3},
  pages={1037-45}
}
We have investigated the effect of several hydrophobic polypeptides on the phase behavior of diacylphosphatidylcholines with different acyl chain length. The polypeptides are uncharged and consist of a sequence with variable length of alternating leucine and alanine, flanked on both sides by two tryptophans, and with the N- and C-termini blocked. First it was demonstrated by circular dichroism measurements that these peptides adopt an alpha-helical conformation with a transmembrane orientation… CONTINUE READING

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