Abstract
We have performed small angle x-ray scattering experiments on a ternary system made of a nonionic surfactant, dodecane, and water, in the absence and upon insertion of a transmembrane protein. In contrast to other proteins or polymers studied, its incorporation reduces the Bragg spacing from 200 Å to 80 Å, which scales as , where c is the protein surface density. The macromolecule incorporated into the hydrophobic part of the lamellar phase appears on freeze-fracture electron micrographs as intramembranous particles. The data are fitted by a simple model of thermally undulating lamellae decorated with protein molecules.
- Received 2 May 1996
DOI:https://doi.org/10.1103/PhysRevLett.77.3485
©1996 American Physical Society