The effects of deimination of myelin basic protein on structures formed by its interaction with phosphoinositide-containing lipid monolayers.

@article{Ishiyama2001TheEO,
  title={The effects of deimination of myelin basic protein on structures formed by its interaction with phosphoinositide-containing lipid monolayers.},
  author={Noboru Ishiyama and Ian R Bates and Christopher M D Hill and Dorothy D Wood and Philip Matharu and Nicholas J. Viner and Mario A. Moscarello and George Harauz},
  journal={Journal of structural biology},
  year={2001},
  volume={136 1},
  pages={30-45}
}
The recombinant 18.5-kDa charge isoform of murine myelin basic protein (rmMBP) is unmodified posttranslationally and was used to study the effects of deimination, i.e., the conversion of arginyl to citrullinyl residues, on the protein's interactions with itself and with lipids. The unmodified species rmMBP-Cit(0) (i.e., containing no citrullinyl residues) interacted with binary monolayers containing acidic (phosphatidylinositol) and nickel-chelating lipids to form paracrystalline arrays with 4… CONTINUE READING