Lipid bilayer polypeptide interactions studied by molecular dynamics simulation.
A model membrane with a polypeptide alpha-helix inserted has been simulated by molecular dynamics at a temperature well above the gel/liquid crystalline phase transition temperature. Order parameters of the lipids and other equilibrium and dynamic quantities have been calculated. Three systems, polyglycine constrained into an alpha-helical configuration, glycophorin with similarly conformationally constrained backbone and finally glycophorin free to change its backbone conformation, have been studied. In all cases there was an ordering of the chains close to the helix. This effect was, however, much smaller for glycophorin with its rather bulky side chains than for polyglycine. The dynamics of the lipids were affected by the neighbouring helix, not drastically however. Lateral diffusion and reorientational time correlations of lipids close to the helix were slower than for the bulk ones, but not more than two or three times. Thus, we did not find any evidence of bound or frozen boundary lipids.
D006021:Glycophorins; D008051:Lipid Bilayers; D008954:Models, Biological; D008968:Molecular Conformation; D010455:Peptides; D011487:Protein Conformation
D006021:Glycophorins; D008051:Lipid Bilayers; D010455:Peptides; C011080:polyglycine