Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes
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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
The secondary structure of lactose permease (I) of Escherichia coli reconstituted in lipid membranes was detd. by Raman spectroscopy. The a-helix content was .apprx.70%, the b-strand content was
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. ...
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 ...
Fluorescence anisotropy measurements on isotropically distributed membranes yield the well-known orientational order parameter as a measure of orientational fluctuations of the fluorophore that are fast compared to the fluorescence lifetime. Measurements o ...
The conformations of melittin, porin, and lactose permease reconstituted in liposomal membranes were investigated by Raman spectroscopy, and the folding of membrane domains was predicted. These data resulted in consistent models for the insertion of the pr ...
Time-resolved fluorescence anisotropy of the single tryptophan (Trp) residue of melittin was measured to assess the orientational fluctuations of the protein in lipid membranes above and below the lipid phase transition temp. (Tt). In phospholipid vesicles ...
Polarized IR spectra of melittin (I) incorporated into macroscopically oriented lipid membranes are reported. From the linear dichroism of the amide I and amide II vibrational bands, the spatial orientation of I helices was detd. as being preferentially pa ...
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 ...
