| Literature DB >> 8612753 |
Abstract
The assembly of two-dimensional membrane protein crystals in the presence of lipids was analyzed with quasielastic light scattering and electron microscopy. Mixtures of detergent-solubilized lipids and/or proteins were submitted to slow or rapid dilution while measuring the hydrodynamic radii of the aggregates. Lipids alone exhibited lambda-shaped dilution curves with intermediate rod-shaped particles that converted into small vesicles. Depending on the protein-protein and protein-lipid interactions, detergent-solubilized protein-lipid mixtures showed a sharp transition from micelles to large densely packed proteoliposomes. Electron microscopy revealed that formation of crystals occurred shortly after this phase transition.Entities:
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Year: 1996 PMID: 8612753 DOI: 10.1016/0014-5793(96)00180-9
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124