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Issue 18, 2010
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Evidence that membrane curvature distorts the tertiary structure of bacteriorhodopsin

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Abstract

The membrane protein bacteriorhodopsin (bR) can be reconstituted into the membrane of the lipid 1-monoolein (MO). This lipid forms a lyotropic liquid crystalline phase whose membrane has hyperbolic interfacial curvature. Using optical absorption spectroscopy and small angle X-ray scattering we have observed retinal unbinding from bR that is correlated with the degree of membrane interfacial curvature. The evidence suggests that bR is susceptible to membrane induced saddle splay for modest perturbations from equilibrium, but for more extreme distortions becomes stiff and resists membrane induced curvature.

Graphical abstract: Evidence that membrane curvature distorts the tertiary structure of bacteriorhodopsin

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Publication details

The article was received on 10 May 2010, accepted on 22 Jul 2010 and first published on 11 Aug 2010


Article type: Communication
DOI: 10.1039/C0SM00353K
Citation: Soft Matter, 2010,6, 4339-4341
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    Evidence that membrane curvature distorts the tertiary structure of bacteriorhodopsin

    C. V. Kulkarni, A. M. Seddon, O. Ces and R. H. Templer, Soft Matter, 2010, 6, 4339
    DOI: 10.1039/C0SM00353K

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