TEMPERATURE-DEPENDENT AGGREGATION OF BACTERIORHODOPSIN IN DIPALMITOYLPHOSPHATIDYLCHOLINE AND DIMYRISTOYLPHOSPHATIDYLCHOLINE VESICLES

被引：155

作者：

CHERRY, RJ

MULLER, U

HENDERSON, R

HEYN, MP

机构：

[1] BIOZENTRUM, DEPT BIOPHYS CHEM, CH-4056 BASEL, SWITZERLAND

[2] MRC, MOLEC BIOL LAB, CAMBRIDGE CB2 2QH, ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1978年 / 121卷 / 02期

关键词：

D O I：

10.1016/S0022-2836(78)80010-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Bacteriorhodopsin has been incorporated into large unilamellar lipid vesicles. Its aggregation behaviour was investigated using X-ray diffraction, electron microscopy, circular dichroism and rotational diffusion measurements. At temperatures below the lipid phase transition, bacteriorhodopsin crystallizes into patches with the same hexagonal lattice observed in the purple membrane. Above the phase transition, the lattice disaggregates and the protein molecules are monomeric provided the lipid to protein ratio is sufficiently high. © 1978 Academic Press Inc. (London) Ltd.

引用

页码：283 / 298

页数：16

共 54 条

[1] EVIDENCE FOR CHROMOPHORE-CHROMOPHORE INTERACTIONS IN PURPLE-MEMBRANE FROM RECONSTITUTION EXPERIMENTS OF CHROMOPHORE-FREE MEMBRANE [J].