Structure and dynamics of crystalline protein layers bound to supported lipid bilayers

We study proteins at the surface of bilayer membranes using streptavidin and avidin bound to biotinylated lipids in a supported lipid bilayer (SLB) at the solid-liquid interface. Using X-ray reflectivity and simultaneous fluorescence microscopy, we characterize the structure and fluidity of protein...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 23(2007), 11 vom: 22. Mai, Seite 6263-9
1. Verfasser: Horton, Margaret R (VerfasserIn)
Weitere Verfasser: Reich, Christian, Gast, Alice P, Rädler, Joachim O, Nickel, Bert
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Fluorescent Dyes Lipid Bilayers Macromolecular Substances Proteins Spin Labels Water 059QF0KO0R Avidin mehr... 1405-69-2 Streptavidin 9013-20-1
Beschreibung
Zusammenfassung:We study proteins at the surface of bilayer membranes using streptavidin and avidin bound to biotinylated lipids in a supported lipid bilayer (SLB) at the solid-liquid interface. Using X-ray reflectivity and simultaneous fluorescence microscopy, we characterize the structure and fluidity of protein layers with varied relative surface coverages of crystalline and noncrystalline protein. With continuous bleaching, we measure a 10-15% decrease in the fluidity of the SLB after the full protein layer is formed. We propose that this reduction in lipid mobility is due to a small fraction (0.04) of immobilized lipids bound to the protein layer that create obstacles to membrane diffusion. Our X-ray reflectivity data show a 40 A thick layer of protein, and we resolve an 8 A layer separating the protein layer from the bilayer. We suggest that the separation provided by this water layer allows the underlying lipid bilayer to retain its fluidity and stability
Beschreibung:Date Completed 11.07.2007
Date Revised 20.11.2014
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827