Identification and characterization of Cu(2)O- and ZnO-binding polypeptides by Escherichia coli cell surface display: toward an understanding of metal oxide binding.

@article{Thai2004IdentificationAC,
  title={Identification and characterization of Cu(2)O- and ZnO-binding polypeptides by Escherichia coli cell surface display: toward an understanding of metal oxide binding.},
  author={Corrine K Thai and Haixia Dai and Manoj R. Sastry and Mehmet Sarikaya and Daniel T. Schwartz and François Baneyx},
  journal={Biotechnology and bioengineering},
  year={2004},
  volume={87 2},
  pages={129-37}
}
We have used the FliTrx cell surface display system to identify disulfide-constrained dodecapeptides binding to the semiconducting metal oxides Cu(2)O and ZnO. Sequence analysis of the inserts revealed that the two populations exhibit similar, yet subtly different patterns of amino acid usage. Both sets of binders were enriched in arginine, tryptophan, and glycine with a higher degree of positional preference in the case of Cu(2)O binders. Tyrosine, proline, and serine were underrepresented in… CONTINUE READING

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