Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium.

@article{Wieprecht1999ThermodynamicsOT,
  title={Thermodynamics of the alpha-helix-coil transition of amphipathic peptides in a membrane environment: implications for the peptide-membrane binding equilibrium.},
  author={Torsten Wieprecht and Ognjan Apostolov and Michael Beyermann and Joachim Seelig},
  journal={Journal of molecular biology},
  year={1999},
  volume={294 3},
  pages={785-94}
}
Amphipathic alpha-helices are the membrane binding motif in many proteins. The corresponding peptides are often random coil in solution but are folded into an alpha-helix upon interaction with the membrane. The energetics of this ubiquitous folding process are still a matter of conjecture. Here, we present a new method to quantitatively analyze the thermodynamics of peptide folding at the membrane interface. We have systematically varied the helix content of a given amphipathic peptide when… CONTINUE READING

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