The orientation of melittin in lipid membranes. A polarized infrared spectroscopy study
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The secondary structure of porin, maltoporin, and OmpA protein reconstituted in lipid membranes was detd. by Raman spectroscopy. The 3 proteins have similar structures consisting of 50-60% b-strand, .apprx.20% b-turn, and
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The effect of melittin on lipid order in dimyristoylphosphatidylcholine bilayers was investigated by Raman spectroscopy and fluorescence anisotropy with diphenylhexatriene as fluorescent probe. In the fluid lipid phase, the Raman results indicated a slight ...
Small-angle neutron scattering data for lipid bilayers in excess water are presented. The method of solvent contrast variation was applied. The variation of scattering intensity with the scattering angle could be analyzed in terms of the model of scatterin ...
The conformation of the polypeptide melittin in lipid membranes as detd. by Raman spectroscopy is a bent a-helix formed by the mainly hydrophobic residues 1-21, and a nonhelical C-terminal segment of the hydrophilic residues 22-26. Fluorescence quenching e ...
Raman spectroscopy and x-ray diffraction are used to investigate the influence of surface charges on the structure of ionizable lipid membranes of dimyristoylmethylphosphatidic acid. The membrane surface charge d. is regulated by varying the pH of the aq. ...
Raman spectroscopy demonstrated that (1) in pure lipid membranes (dihexadecylphosphatidic acid or phosphatidylcholines), the lipid chains are mainly in an all-trans conformation in the ordered membrane phase, and in the fluid phase, lipid chains contain al ...
CD and fluorescence were used to study the interaction of the model peptide melittin with dimyristoylphosphatidylcholine (DMPC) bilayer liposomes. Melittin binds tightly to the lipid membrane and undergoes a conformational change from a random to an .apprx ...
