pH triggered self-assembly of native and recombinant amelogenins under physiological pH and temperature in vitro.

@article{WiedemannBidlack2007pHTS,
  title={pH triggered self-assembly of native and recombinant amelogenins under physiological pH and temperature in vitro.},
  author={Felicitas B. Wiedemann-Bidlack and Elia Beniash and Yasuo Yamakoshi and James P. Simmer and Henry C. Margolis},
  journal={Journal of structural biology},
  year={2007},
  volume={160 1},
  pages={57-69}
}
Self-assembly of the extracellular matrix protein amelogenin is believed to play an essential role in regulating the growth and organization of enamel crystals during enamel formation. This study examines the effect of temperature and pH on amelogenin self-assembly under physiological pH conditions in vitro, using dynamic light scattering, turbidity measurements, and transmission electron microscopy. Full-length recombinant amelogenins from mouse (rM179) and pig (rP172) were investigated, along… CONTINUE READING

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