Olivier Soubias

TL;DR: It is concluded that spectral broadening arises from composition fluctuations in the membrane plane with dimensions of <50 nm and speculate that similar fluctuations are commonly found in cholesterol-containing membranes.

TL;DR: Three all-atom molecular dynamics simulations predict that substantial changes in internal hydration play a functional role in rhodopsin activation, and confirm with (1)H magic angle spinning NMR that the increased hydration is specific to the metarhodopin-I intermediate.

TL;DR: The experiments point to the importance of interactions of rhodopsin with particular lipid species in the first layer of lipids surrounding the protein as well as to membrane elastic stress in the lipid-protein domain.

TL;DR: The experiments show clearly that the surface of rhodopsin has sites for specific interaction with lipids, and current theories of lipid-protein interaction do not account for such surface heterogeneity.

TL;DR: A variety of mechanisms seems to be responsible for the large, lipid-induced shifts between MI and MII: adjustment of the thickness of lipid bilayers to rhodopin and adjustment of rhodopsin helicity to the Thickness of bilayers, curvature elastic deformations in the lipid matrix surrounding the protein, direct interactions of PE headgroups and polyunsaturated hydrocarbon chains with rhodOPSin, and direct or lipid-mediated interactions between r Rhodopsin molecules.