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- W2080989693 abstract "Solid-state 31P- and 13C-NMR spectra were recorded in melittin-lecithin vesicles composed of 1,2-dilauroyl-sn-glycero-3-phosphocholine (DLPC) or 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC). Highly ordered magnetic alignments were achieved with the membrane surface parallel to the magnetic field above the gel-to-liquid crystalline phase transition temperature (Tc). Using these magnetically oriented vesicle systems, dynamic structures of melittin bound to the vesicles were investigated by analyzing the 13C anisotropic and isotropic chemical shifts of selectively 13C-labeled carbonyl carbons of melittin under the static and magic-angle spinning conditions. These results indicate that melittin molecules adopt an α-helical structure and laterally diffuse to rotate rapidly around the membrane normal with tilt angles of the N-terminal helix being −33° and −36° and those of the C-terminal helix being 21° and 25° for DLPC and DPPC vesicles, respectively. The rotational-echo double-resonance method was used to measure the interatomic distance between [1-13C]Val8 and [15N]Leu13 to further identify the bending α-helical structure of melittin to possess the interhelical angles of 126° and 119° in DLPC and DPPC membranes, respectively. These analyses further lead to the conclusion that the α-helices of melittin molecules penetrate the hydrophobic cores of the bilayers incompletely as a pseudo-trans-membrane structure and induce fusion and disruption of vesicles." @default.
- W2080989693 created "2016-06-24" @default.
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- W2080989693 date "2004-11-01" @default.
- W2080989693 modified "2023-10-16" @default.
- W2080989693 title "Dynamic Structure of Vesicle-Bound Melittin in a Variety of Lipid Chain Lengths by Solid-State NMR" @default.
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- W2080989693 doi "https://doi.org/10.1529/biophysj.104.046102" @default.
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