Stable self-assembly of a protein engineering scaffold on gold surfaces.

@article{Terrettaz2002StableSO,
  title={Stable self-assembly of a protein engineering scaffold on gold surfaces.},
  author={Samuel Terrettaz and Wolf-Peter Ulrich and Horst Vogel and Qi Hong and Lynn George Dover and Jeremy H Lakey},
  journal={Protein science : a publication of the Protein Society},
  year={2002},
  volume={11 8},
  pages={1917-25}
}
The outer membrane protein OmpF from Escherichia coli is a member of a large family of beta-barrel membrane proteins. Some, like OmpF, are pore-forming proteins whilse others are active transporters or enzymes. We have previously shown that the receptor-binding domain (R-domain) of the toxin colicin N binds with high affinity to OmpF reconstituted into tethered lipid bilayers on gold electrodes. The binding can be measured by surface plasmon resonance (SPR) and ion channel blockage (impedance… CONTINUE READING