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• W2013894497 abstract "Low-angle and wide-angle X-ray scattering data from phosphatidylglycerol complexed with myelin basic protein, poly(L-lysine) and calcium ions are analyzed. The results confirm our earlier report (Brady, G.W., Murthy, N.S., Fein, D.B., Wood, D.D. and Moscarello, M.A. (1981) Biophys. J. 34, 345-350) that the basic protein interacts primarily with the polar headgroups of the lipid; and that at high protein concentrations (greater than 35%) the bilayers aggregate to form multilayers with a repeat period of 68 A, the single bilayer to multilayer transition being a cooperative process. Polylysine and Ca2+ produce multilayers with a smaller repeat of approx. 55 A. Basic protein and polylysine do not change the fluid-like arrangement of the hydrocarbon chains (diffuse 4.6 A peak in the wide-angle pattern), whereas Ca2+ probably induces a two-dimensional order (4.3 A and 3.9 A peak in the wide-angle pattern). Electron density profiles of the lipid and lipid-basic protein vesicles indicate that the basic protein penetrates into the bilayer." @default.
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• W2013894497 date "1984-01-01" @default.
• W2013894497 modified "2023-09-24" @default.
• W2013894497 title "X-ray scattering studies of a model complex of lipid and basic protein of myelin" @default.
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• W2013894497 doi "https://doi.org/10.1016/0005-2736(84)90335-3" @default.
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