Structure and polymorphism of the hydrocarbon chains of lipids: A study of lecithin-water phases

Tardieu, A.; Luzzati, Vittorio; Reman, F.C.

doi:10.1016/0022-2836(73)90303-3

Cited by 1,228 publications

(857 citation statements)

References 27 publications

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“…The 4-maleimido-derivative of Tempo [2,2,6,6-tetramethylpiperidine-l-oxyl, made according to the general procedure described by Griffith and McConnell (18) (19)(20)(21)(22)(23)(24)(25), and these patterns can sometimes be used to distinguish fluid from rigid lipid regions (24)(25)(26). are on the order of 40 A in diameter (uncorrected for shadow thickness).…”

Section: Methodsmentioning

confidence: 99%

Glycophorin in Lipid Bilayers

Grant¹,

McConnell²

1974

Proc. Natl. Acad. Sci. U.S.A.

147

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Glycophorin, the major glycoprotein of human erythrocytes, has been isolated and reincorporated into lipid vesicles. Freeze-fracture electron microscopy shows the reincorporated glycophorin to occur as small particles in vesicle fracture faces while the etch faces are smooth. The glycoprotein has a tendency to cluster into groups of several particles. Evidence is presented that, although lipids in immediate contact with glycophcrin are likely somewhat immobilized, the entire lipid-piotein complex has a tendency to occupy fluid regions of the bilayer. Reincorporated glycophorin assumes its proposed conformation in the intact erythrocyte in so far as it penetrates the hydrophobic membrane interior while its N-terminal end with attached carbohydrate residues is exposed to the aqueous compartment and is available as a specific recognition site.

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Section: Methodsmentioning

confidence: 99%

Glycophorin in Lipid Bilayers

Grant¹,

McConnell²

1974

Proc. Natl. Acad. Sci. U.S.A.

147

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“…The experimental data suggest that this may not necessarily be correct. Using an effective volume of 27-0 A 3 for the CH 2 group (Tardieu et al 1973) one calculates a microviscosity of 17 ct 13 cP (at 51 °C) for the rotational friction in the plateau region of the DPPC bilayer. The rotational microviscosity estimated from "C-nmr relaxation times is c. 50 cP (Lee et al 1976).…”

Section: Phospholipid Dynamics and Membrane Fluiditymentioning

confidence: 99%

“…V. Luzzati was also the first to emphasize the liquid-like conformation of the hydrocarbon chains, similar to that of a liquid paraffin, yet with the average orientation of the chains perpendicular to the lipid-water interface. This liquid-crystalline bilayer is generally observed in lipidwater systems at sufficiently high temperature and water content, as well as in intact biological membranes under physiological conditions (Luzzati & Husson, 1962;Luzzati, 1968;Tardieu, Luzzati & Reman, 1973;Engelman, 1971;Shipley, 1973). In combination with thermodynamic and other spectroscopic observations these investigations culminated in the formulation of the fluid mosaic model of biological membranes (cf.…”

mentioning

confidence: 93%

Lipid conformation in model membranes and biological membranes

Seelig

1980

Quart. Rev. Biophys.

798

443

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Protein molecules in solution or in protein crystals are characterized by rather well-defined structures in which α-helical regions, β-pleated sheets, etc., are the key features. Likewise, the double helix of nucleic acids has almost become the trademark of molecular biology as such. By contrast, the structural analysis of lipids has progressed at a relatively slow pace. The early X-ray diffraction studies by V. Luzzati and others firmly established the fact that the lipids in biological membranes are predominantly organized in bilayer structures (Luzzati, 1968). V. Luzzati was also the first to emphasize the liquid-like conformation of the hydrocarbon chains, similar to that of a liquid paraffin, yet with the average orientation of the chains perpendicular to the lipid–water interface. This liquid–crystalline bilayer is generally observed in lipid–water systems at sufficiently high temperature and water content, as well as in intact biological membranes under physiological conditions (Luzzati & Husson, 1962; Luzzati, 1968; Tardieu, Luzzati & Reman, 1973; Engelman, 1971; Shipley, 1973). In combination with thermodynamic and other spectroscopic observations these investigations culminated in the formulation of the fluid mosaic model of biological membranes (cf. Singer, 1971). However, within the limits of this model the exact nature of lipid conformation and dynamics was immaterial, the lipids were simply pictured as circles with two squiggly lines representing the polar head group and the fatty acyl chains, respectively. No attempt was made to incorporate the well-established chemical structure into this picture. Similarly, membrane proteins were visualized as smooth rotational ellipsoids disregarding the possibility that protruding amino acid side-chains and irregularities of the backbone folding may create a rather rugged protein surface.

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“…It was 50/~m in our measurements and therefore assumption (3) does not seem to cause a serious error. Table 1 of the article by Tardieu, Luzzati & Reman (1973) gives values of the cross-sectional area S and the tilting angle of the hydrocarbon chain with respect to the membrane surface in the dipalmitoyl lecithin bilayer at various water contents. The value of S (43.7 A z) obtained for our uranyl-decorated lecithin bilayer is closer to the value (42.7 A 2) at low water content than the value (48.6 A 2) at high water content given in their table.…”

Section: Discussionmentioning

confidence: 99%

Structures of uranyl-decorated lecithin and lecithin–cholesterol bilayers

K¹,

Yamaguchi²,

Inoko³

et al. 1976

Acta Crystallogr Sect B

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Dipalmitoyl lecithin and dipalmitoyl lecithin-cholesterol bilayers are capable of binding about the same number of uranyl ions as lecithin molecules. Dispersions of the uranyl-decorated bilayers give very distinct continuous X-ray diffraction peaks up to the seventh order. Electron density projection onto the normal to the membrane is obtained with a resolution of about 6.5 ~. It gives two high peaks separated by 48/~, indicating that uranyl ions are bound at the surfaces of membranes in both lecithin and lecithin--cholesterol bilayers.

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Structure and polymorphism of the hydrocarbon chains of lipids: A study of lecithin-water phases

Cited by 1,228 publications

References 27 publications

Glycophorin in Lipid Bilayers

Glycophorin in Lipid Bilayers

Lipid conformation in model membranes and biological membranes

Structures of uranyl-decorated lecithin and lecithin–cholesterol bilayers

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