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Protein lateral distribution in lipid bilayer membranes. Applications to ESR studies.

作者信息

Laidlaw D J, Pink D A

出版信息

Eur Biophys J. 1985;12(3):143-51. doi: 10.1007/BF00254072.

DOI:10.1007/BF00254072
PMID:2995020
Abstract

We analyse recent ESR measurements on Ca2+ ATPase and Myelin proteolipid apoprotein reconstituted in phosphatidylcholine bilayer membranes. Our intention is to discover whether the measurements indicate significant protein-protein repulsive or attractive interactions. In order to do so we have studied a model of a lipid bilayer membrane containing transbilayer proteins. It represents the proteins by hexagons moving on a triangular lattice interacting via an energy E0 which can be attractive, repulsive or zero. The last-named represents that all of the Ca2+ ATPase data is best described either by the "random" model or, possibly, by one in which there is a small repulsive interaction, but not by the "annulus" model or one in which there is always at least one layer of lipid chains between every pair of proteins. We find that all of the Myelin PLA data is best described by a "random" distribution of hexamers and not by an "annulus" model of hexamers. We suggest measurements that can be done in order to unambiguously settle the question of whether these systems are best described by a "random"-type model or an "annulus"-type model.

摘要

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引用本文的文献

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本文引用的文献

1
Theoretical studies of phospholipid bilayers and monolayers. Perturbing probes, monolayer phase transitions, and computer simulations of lipid-protein bilayers.磷脂双层和单层的理论研究。扰动探针、单层相变以及脂蛋白双层的计算机模拟。
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Competition between cholesterol and phosphatidylcholine for the hydrophobic surface of sarcoplasmic reticulum Ca2+-ATPase.
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Rotational dynamics of protein and boundary lipid in sarcoplasmic reticulum membrane.肌质网膜中蛋白质与边界脂质的旋转动力学
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Stoichiometry and specificity of lipid-protein interaction with myelin proteolipid protein studied by spin-label electron spin resonance.通过自旋标记电子自旋共振研究髓鞘蛋白脂蛋白中脂质 - 蛋白质相互作用的化学计量学和特异性。
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Biochemistry. 1979 Oct 16;18(21):4480-7. doi: 10.1021/bi00588a005.