Home > Publications database > The Protein Tethered Lipid Bilayer - a novel mimic of the biological membrane |
Journal Article | PreJuSER-41694 |
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2004
Rockefeller Univ. Press
New York, NY
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Please use a persistent id in citations: http://hdl.handle.net/2128/700 doi:10.1529/biophysj.104.046169
Abstract: A new concept of solid-supported tethered bilayer lipid membrane (tBLM) for the functional incorporation of membrane proteins is introduced. The incorporated protein itself acts as the tethering molecule resulting in a versatile system in which the protein determines the characteristics of the submembraneous space. This architecture is achieved through a metal chelating surface, to which histidine-tagged (His-tagged) membrane proteins are able to bind in a reversible manner. The tethered bilayer lipid membrane is generated by substitution of protein-bound detergent molecules with lipids using in-situ dialysis or adsorption. The system is characterized by surface plasmon resonance, quartz crystal microbalance, and electrochemical impedance spectroscopy. His-tagged cytochrome c oxidase (CcO) is used as a model protein in this study. However, the new system should be applicable to all recombinant membrane proteins bearing a terminal His-tag. In particular, combination of surface immobilization and membrane reconstitution opens new prospects for the investigation of functional membrane proteins by various surface-sensitive techniques under a defined electric field.
Keyword(s): Biomimetics: methods (MeSH) ; Cell Membrane: chemistry (MeSH) ; Electric Impedance (MeSH) ; Electron Transport Complex IV: chemistry (MeSH) ; Histidine: chemistry (MeSH) ; Lipid Bilayers: chemistry (MeSH) ; Macromolecular Substances (MeSH) ; Membrane Fluidity (MeSH) ; Membrane Proteins: chemistry (MeSH) ; Membranes, Artificial (MeSH) ; Molecular Conformation (MeSH) ; Protein Binding (MeSH) ; Lipid Bilayers ; Macromolecular Substances ; Membrane Proteins ; Membranes, Artificial ; Histidine ; Electron Transport Complex IV ; J
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