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001 | 41694 | ||
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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 |
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024 | 7 | _ | |a 2128/700 |2 Handle |
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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 |2 DataCite |
336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
336 | 7 | _ | |a ARTICLE |2 BibTeX |
336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
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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