This title appears in the Scientific Report :
2004
Please use the identifier:
http://dx.doi.org/10.1529/biophysj.104.046169 in citations.
Please use the identifier: http://hdl.handle.net/2128/700 in citations.
The Protein Tethered Lipid Bilayer - a novel mimic of the biological membrane
The Protein Tethered Lipid Bilayer - a novel mimic of the biological membrane
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 subme...
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Personal Name(s): | Gieß, F. |
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Friedrich, M. / Heberle, J. / Naumann, R. / Knoll, W. | |
Contributing Institute: |
Biologische Strukturforschung; IBI-2 |
Published in: | Biophysical journal, 87 (2004) S. 3213 - 3220 |
Imprint: |
New York, NY
Rockefeller Univ. Press
2004
|
Physical Description: |
3213 - 3220 |
DOI: |
10.1529/biophysj.104.046169 |
PubMed ID: |
15339795 |
Document Type: |
Journal Article |
Research Program: |
Neurowissenschaften |
Series Title: |
Biophysical Journal
87 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/700 in citations.
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. |