%0 Journal Article
%A Gieß, F.
%A Friedrich, M.
%A Heberle, J.
%A Naumann, R.
%A Knoll, W.
%T The Protein Tethered Lipid Bilayer - a novel mimic of the biological membrane
%J Biophysical journal
%V 87
%@ 0006-3495
%C New York, NY
%I Rockefeller Univ. Press
%M PreJuSER-41694
%P 3213 - 3220
%D 2004
%Z Record converted from VDB: 12.11.2012
%X 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.
%K Biomimetics: methods
%K Cell Membrane: chemistry
%K Electric Impedance
%K Electron Transport Complex IV: chemistry
%K Histidine: chemistry
%K Lipid Bilayers: chemistry
%K Macromolecular Substances
%K Membrane Fluidity
%K Membrane Proteins: chemistry
%K Membranes, Artificial
%K Molecular Conformation
%K Protein Binding
%K Lipid Bilayers (NLM Chemicals)
%K Macromolecular Substances (NLM Chemicals)
%K Membrane Proteins (NLM Chemicals)
%K Membranes, Artificial (NLM Chemicals)
%K Histidine (NLM Chemicals)
%K Electron Transport Complex IV (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:15339795
%2 pmc:PMC1304791
%U <Go to ISI:>//WOS:000224732500026
%R 10.1529/biophysj.104.046169
%U https://juser.fz-juelich.de/record/41694