001     41694
005     20200423203926.0
017 _ _ |a This version is available at the following Publisher URL: http://www.biophysj.org/
024 7 _ |a pmid:15339795
|2 pmid
024 7 _ |a pmc:PMC1304791
|2 pmc
024 7 _ |a 10.1529/biophysj.104.046169
|2 DOI
024 7 _ |a WOS:000224732500026
|2 WOS
024 7 _ |a 2128/700
|2 Handle
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|2 altmetric
037 _ _ |a PreJuSER-41694
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biophysics
100 1 _ |a Gieß, F.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a The Protein Tethered Lipid Bilayer - a novel mimic of the biological membrane
260 _ _ |a New York, NY
|b Rockefeller Univ. Press
|c 2004
300 _ _ |a 3213 - 3220
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biophysical Journal
|x 0006-3495
|0 882
|v 87
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Biomimetics: methods
650 _ 2 |2 MeSH
|a Cell Membrane: chemistry
650 _ 2 |2 MeSH
|a Electric Impedance
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: chemistry
650 _ 2 |2 MeSH
|a Histidine: chemistry
650 _ 2 |2 MeSH
|a Lipid Bilayers: chemistry
650 _ 2 |2 MeSH
|a Macromolecular Substances
650 _ 2 |2 MeSH
|a Membrane Fluidity
650 _ 2 |2 MeSH
|a Membrane Proteins: chemistry
650 _ 2 |2 MeSH
|a Membranes, Artificial
650 _ 2 |2 MeSH
|a Molecular Conformation
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 7 |0 0
|2 NLM Chemicals
|a Lipid Bilayers
650 _ 7 |0 0
|2 NLM Chemicals
|a Macromolecular Substances
650 _ 7 |0 0
|2 NLM Chemicals
|a Membrane Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Membranes, Artificial
650 _ 7 |0 71-00-1
|2 NLM Chemicals
|a Histidine
650 _ 7 |0 EC 1.9.3.1
|2 NLM Chemicals
|a Electron Transport Complex IV
650 _ 7 |a J
|2 WoSType
700 1 _ |a Friedrich, M.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Heberle, J.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB572
700 1 _ |a Naumann, R.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Knoll, W.
|b 4
|0 P:(DE-HGF)0
773 _ _ |a 10.1529/biophysj.104.046169
|g Vol. 87, p. 3213 - 3220
|p 3213 - 3220
|q 87<3213 - 3220
|0 PERI:(DE-600)1477214-0
|t Biophysical journal
|v 87
|y 2004
|x 0006-3495
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1304791
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