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000041694 0247_ $$2pmc$$apmc:PMC1304791
000041694 0247_ $$2DOI$$a10.1529/biophysj.104.046169
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000041694 084__ $$2WoS$$aBiophysics
000041694 1001_ $$0P:(DE-HGF)0$$aGieß, F.$$b0
000041694 245__ $$aThe Protein Tethered Lipid Bilayer - a novel mimic of the biological membrane
000041694 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2004
000041694 300__ $$a3213 - 3220
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000041694 440_0 $$0882$$aBiophysical Journal$$v87$$x0006-3495
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000041694 520__ $$aA new concept of solid-supported tethered bilayer lipid membrane (tBLM) for the functional incorporation of membrane proteins is introduced. The incorporated protein itself acts as the tethering molecule resulting in a versatile system in which the protein determines the characteristics of the submembraneous space. This architecture is achieved through a metal chelating surface, to which histidine-tagged (His-tagged) membrane proteins are able to bind in a reversible manner. The tethered bilayer lipid membrane is generated by substitution of protein-bound detergent molecules with lipids using in-situ dialysis or adsorption. The system is characterized by surface plasmon resonance, quartz crystal microbalance, and electrochemical impedance spectroscopy. His-tagged cytochrome c oxidase (CcO) is used as a model protein in this study. However, the new system should be applicable to all recombinant membrane proteins bearing a terminal His-tag. In particular, combination of surface immobilization and membrane reconstitution opens new prospects for the investigation of functional membrane proteins by various surface-sensitive techniques under a defined electric field.
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000041694 650_2 $$2MeSH$$aBiomimetics: methods
000041694 650_2 $$2MeSH$$aCell Membrane: chemistry
000041694 650_2 $$2MeSH$$aElectric Impedance
000041694 650_2 $$2MeSH$$aElectron Transport Complex IV: chemistry
000041694 650_2 $$2MeSH$$aHistidine: chemistry
000041694 650_2 $$2MeSH$$aLipid Bilayers: chemistry
000041694 650_2 $$2MeSH$$aMacromolecular Substances
000041694 650_2 $$2MeSH$$aMembrane Fluidity
000041694 650_2 $$2MeSH$$aMembrane Proteins: chemistry
000041694 650_2 $$2MeSH$$aMembranes, Artificial
000041694 650_2 $$2MeSH$$aMolecular Conformation
000041694 650_2 $$2MeSH$$aProtein Binding
000041694 650_7 $$00$$2NLM Chemicals$$aLipid Bilayers
000041694 650_7 $$00$$2NLM Chemicals$$aMacromolecular Substances
000041694 650_7 $$00$$2NLM Chemicals$$aMembrane Proteins
000041694 650_7 $$00$$2NLM Chemicals$$aMembranes, Artificial
000041694 650_7 $$071-00-1$$2NLM Chemicals$$aHistidine
000041694 650_7 $$0EC 1.9.3.1$$2NLM Chemicals$$aElectron Transport Complex IV
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000041694 7001_ $$0P:(DE-HGF)0$$aFriedrich, M.$$b1
000041694 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b2$$uFZJ
000041694 7001_ $$0P:(DE-HGF)0$$aNaumann, R.$$b3
000041694 7001_ $$0P:(DE-HGF)0$$aKnoll, W.$$b4
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000041694 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1304791
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