Increased stability upon heptamerization of the pore-forming toxin aerolysin.

@article{Lesieur1999IncreasedSU,
  title={Increased stability upon heptamerization of the pore-forming toxin aerolysin.},
  author={Claire Lesieur and Severine Frutiger and Gillian Hughes and Roland Kellner and Franc Pattus and F Gisou van der Goot},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 51},
  pages={36722-8}
}
Aerolysin is a bacterial pore-forming toxin that is secreted as an inactive precursor, which is then processed at its COOH terminus and finally forms a circular heptameric ring which inserts into membranes to form a pore. We have analyzed the stability of the precursor proaerolysin and the heptameric complex. Equilibrium unfolding induced by urea and guanidinium hydrochloride was monitored by measuring the intrinsic tryptophan fluorescence of the protein. Proaerolysin was found to unfold in two… CONTINUE READING

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