PMID- 15339795
OWN - NLM
STAT- MEDLINE
DCOM- 20050325
LR  - 20181113
IS  - 0006-3495 (Print)
IS  - 1542-0086 (Electronic)
IS  - 0006-3495 (Linking)
VI  - 87
IP  - 5
DP  - 2004 Nov
TI  - The protein-tethered lipid bilayer: a novel mimic of the biological membrane.
PG  - 3213-20
AB  - 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.
FAU - Giess, Frank
AU  - Giess F
AD  - Max Planck Institute for Polymer Research, Mainz, Germany.
FAU - Friedrich, Marcel G
AU  - Friedrich MG
FAU - Heberle, Joachim
AU  - Heberle J
FAU - Naumann, Renate L
AU  - Naumann RL
FAU - Knoll, Wolfgang
AU  - Knoll W
LA  - eng
PT  - Journal Article
DEP - 20040831
PL  - United States
TA  - Biophys J
JT  - Biophysical journal
JID - 0370626
RN  - 0 (Lipid Bilayers)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Membrane Proteins)
RN  - 0 (Membranes, Artificial)
RN  - 4QD397987E (Histidine)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Biomimetics/*methods
MH  - Cell Membrane/*chemistry
MH  - Electric Impedance
MH  - Electron Transport Complex IV/*chemistry
MH  - Histidine/*chemistry
MH  - Lipid Bilayers/*chemistry
MH  - Macromolecular Substances
MH  - Membrane Fluidity
MH  - Membrane Proteins/*chemistry
MH  - Membranes, Artificial
MH  - Molecular Conformation
MH  - Protein Binding
PMC - PMC1304791
EDAT- 2004/09/02 05:00
MHDA- 2005/03/26 09:00
PMCR- 2005/11/01
CRDT- 2004/09/02 05:00
PHST- 2004/09/02 05:00 [pubmed]
PHST- 2005/03/26 09:00 [medline]
PHST- 2004/09/02 05:00 [entrez]
PHST- 2005/11/01 00:00 [pmc-release]
AID - S0006-3495(04)73790-X [pii]
AID - 46169 [pii]
AID - 10.1529/biophysj.104.046169 [doi]
PST - ppublish
SO  - Biophys J. 2004 Nov;87(5):3213-20. doi: 10.1529/biophysj.104.046169. Epub 2004 
      Aug 31.