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Biointerphases

Journal for Biophysical Chemistry

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Protein tethered lipid bilayer: An alternative mimic of the biological membrane (Mini Review)

Biointerphases volume 3, pages FA101–FA107 (2008)Cite this article

Abstract

An overview is given about results obtained so far with an alternative concept of solid-supported tethered lipid bilayers for the functional incorporation of membrane proteins. The incorporated protein itself acts as the tethering molecule resulting in a versatile system where the protein determines the characteristics of submembraneous space. This architecture is achieved through a metal chelating surface, onto which histidine-tagged (his-tagged) membrane proteins are able to bind in a reversible manner. The tethered bilayer membrane is generated by substitution of protein bund detergent molecules with lipids using in situ dialysis or adsorption. Histidine-tagged ctochrome c oxidase is used as a model protein in this study. However, the system should be applicable to all recombinant membrane proteins bearing a terminal his tag. The system is particularly designed, among other surface-analytical techniques, for a combined application of electrochemical and vibrational spectroscopy measurements.

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Authors and Affiliations

  1. Max Planck Institute for Polymer Research, 55128, Mainz, Germany

    Renate L. C. Naumann & Wolfgang Knoll

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  1. Renate L. C. Naumann
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  2. Wolfgang Knoll
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Naumann, R.L.C., Knoll, W. Protein tethered lipid bilayer: An alternative mimic of the biological membrane (Mini Review). Biointerphases 3, FA101–FA107 (2008). https://doi.org/10.1116/1.2936939

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  • DOI: https://doi.org/10.1116/1.2936939