Interactions of alpha-helices with lipid bilayers: a review of simulation studies

摘要: Membrane proteins, of which the majority seem to contain one or more alpha-helix, constitute approx. 30% most genomes. A complete understanding nature helix/bilayer interactions is necessary for an structural principles underlying membrane proteins. This review describes computer simulation studies interactions. Key experimental alpha-helices and lipid bilayers are briefly reviewed. Surface associated helices found in some membrane-bound enzymes (e.g. prostaglandin synthase), as stages mechanisms antimicrobial peptides pore-forming bacterial toxins. Transmembrane integral also channels formed by amphipathic Mean field simulations, bilayer approximated a hydrophobic continuum, have been used membrane-active alamethicin, melittin, magainin dermaseptin) simple proteins phage Pf1 coat protein). All atom molecular dynamics simulations fully solvated with transmembrane applied to: constituent bacteriorhodopsin; peptide-16 (a model TM helix); number pore-lining from ion channels. melittin simulated, alpha-helical bundles such bacteriorhodopsin alamethicin. From comparison results two classes simulation, it emerges that major theoretical challenge exploit all order improve mean approach.