Models for the structure of outer-membrane proteins of Escherichia coli derived from raman spectroscopy and prediction methods.

@article{Vogel1986ModelsFT,
  title={Models for the structure of outer-membrane proteins of Escherichia coli derived from raman spectroscopy and prediction methods.},
  author={Horst Vogel and Fritz J{\"a}hnig},
  journal={Journal of molecular biology},
  year={1986},
  volume={190 2},
  pages={191-9}
}
The secondary structure of porin, maltoporin and OmpA protein reconstituted in lipid membranes is determined by Raman spectroscopy. The three proteins have similar structures consisting of 50 to 60% beta-strand, about 20% beta-turn, and less than 15% alpha-helix. Employing a method for structural prediction that accounts for amphipathic beta-strands, folding models are developed for porin and for the segment of OmpA protein incorporated into the membrane. In the model, the OmpA fragment… CONTINUE READING

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