Refolding of bacteriorhodopsin from expressed polypeptide fragments.

@article{Marti1998RefoldingOB,
  title={Refolding of bacteriorhodopsin from expressed polypeptide fragments.},
  author={Thomas Marti},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 15},
  pages={9312-22}
}
  • Thomas Marti
  • Published 1998 in The Journal of biological chemistry
Bacteriorhodopsin is a heptahelical membrane protein that can be refolded to the native state following denaturation. To analyze the in vitro folding process with independent structural domains, eight fragments comprising two (AB, FG), three (AC, EG), four (AD, DG) or five (AE, CG) of the transmembrane segments were produced by expression in Escherichia coli. The polypeptides were purified to homogeneity by solvent extraction of E. coli membranes, repeated phase separation, and anion-exchange… CONTINUE READING

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