The role of retinal in the long-range protein-lipid interactions in bacteriorhodopsin-phosphatidylcholine vesicles

@article{Bryl2000TheRO,
  title={The role of retinal in the long-range protein-lipid interactions in bacteriorhodopsin-phosphatidylcholine vesicles},
  author={Krzysztof Bryl and Kazuo Yoshihara},
  journal={European Biophysics Journal},
  year={2000},
  volume={29},
  pages={628-640}
}
The effects of bacteriorhodopsin analogues and the analogues of a bacteriorhodopsin mutant (D96N) on the lateral organization of lipids have been investigated with lipid species with a variety of acyl chain lengths. The analogues, obtained by regeneration of bacterioopsin or mutant opsin with 14-, 12-, 10-, or 8-fluororetinal, were reconstituted with 1,2-didodecanoyl-sn-glycero-3-phosphocholine, 1,2-ditetradecanoyl-sn-glycero-3-phosphocholine, 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine, and… CONTINUE READING

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The role of retinal in the long - range protein - lipid interactions in bacteriorhodopsin - phosphatidylcholine vesicles .
Evidence was provided that retinal contributed to the long - range protein - lipid interactions in bacteriorhodopsin - phosphatidylcholine vesicles .
Evidence was provided that retinal contributed to the long - range protein - lipid interactions in bacteriorhodopsin - phosphatidylcholine vesicles .
The role of retinal in the long - range protein - lipid interactions in bacteriorhodopsin - phosphatidylcholine vesicles .
Evidence was provided that retinal contributed to the long - range protein - lipid interactions in bacteriorhodopsin - phosphatidylcholine vesicles .
The role of retinal in the long - range protein - lipid interactions in bacteriorhodopsin - phosphatidylcholine vesicles .
The substitution of retinal with 14-fluororetinal resulted in much stronger effects of the protein on the lipids : a more pronounced up - shift of the lipid phase transition temperature , a rigidifying effect on all the lipids used , and an elongation of the distance over which the hydrophobic thickness of the lipid bilayer was perturbed by the protein .
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