Secondary structure and orientation of the pore-forming toxin lysenin in a sphingomyelin-containing membrane.

@article{Here2008SecondarySA,
  title={Secondary structure and orientation of the pore-forming toxin lysenin in a sphingomyelin-containing membrane.},
  author={Monika Here{\'c} and Mariusz Gagoś and Magdalena Kulma and Katarzyna Kwiatkowska and Andrzej Sobota and Wieslaw I Gruszecki},
  journal={Biochimica et biophysica acta},
  year={2008},
  volume={1778 4},
  pages={872-9}
}
Lysenin is a sphingomyelin-recognizing toxin which forms stable oligomers upon membrane binding and causes cell lysis. To get insight into the mechanism of the transition of lysenin from a soluble to a membrane-bound form, surface activity of the protein and its binding to lipid membranes were studied using tensiometric measurements, Fourier-transform infrared spectroscopy (FTIR) and FTIR-linear dichroism. The results showed cooperative adsorption of recombinant lysenin-His at the argon-water… CONTINUE READING