Philippe Ducarme

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The lipid bilayer is crucial for the folding of integral membrane proteins. This article presents an empirical method to account for water-lipid interfaces in the insertion of molecules interacting with bilayers. The interactions between the molecule and the bilayer are described by restraint functions designed to mimic the membrane effect. These functions(More)
The cystic fibrosis transmembrane conductance regulator is a cAMP-regulated chloride channel. We used molecular modelling to predict 3-D models for the CFTR membrane domain. Hydropathy and residue conservation in all CFTRs as well as in other proteins suggested that the membrane domain is a 12-helix bundle. If the domain is enclosing a channel for chloride,(More)
In order to better understand the driving forces that determine the alignment of amphipathic helical polypeptides with respect to the surface of phospholipid bilayers, lysine-containing peptide sequences were designed, prepared by solid-phase chemical synthesis, and reconstituted into membranes. CD spectroscopy indicates that all peptides exhibit a high(More)
Nisin is a 34-residue lantibiotic widely used as food preservative. Its mode of action on the bacterial cytoplasmic membrane is unclear. It should form ion channels but a molecular description of the interaction between nisin and phospholipids is lacking. The interactions between nisin and a membrane and the influence of phospholipids are here analysed by(More)
A continuous membrane model (IMPALA) was previously developed to predict how hydrophobic spans of proteins insert in membranes (Mol. Mod. 2 (1996) 27). Using that membrane model, we looked for the interactions between several hydrophobic spans. We used the glycophorin A dimer as an archetype of polytopic protein to validate the approach. We find that the(More)
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