| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10429793 | Biosensors and Bioelectronics | 2005 | 4 Pages |
Abstract
When LacP was reconstituted in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) liposomes, the proteolipid sheets were densely packed with an upper layer that protruded from a background layer. Several lipid protein molar ratios (LPR) were screened. High resolution analysis of the upper layer revealed a quasi-crystalline arrangement formed by small entities that could be attributed to the protein. The approach described here may be suitable for the rational design of biosensors based in other transmembrane proteins.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Sandra Merino, Ãscar Domènech, M.Teresa Montero, Jordi Hernández-Borrell,