Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains.

@article{Michenfelder2003CharacterizationOT,
  title={Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains.},
  author={Martina Michenfelder and Germaine Fu and Camille Lawrence and James C. Weaver and Brandon A Wustman and Laura Taranto and John Spencer Evans and Daniel E Morse},
  journal={Biopolymers},
  year={2003},
  volume={70 4},
  pages={522-33}
}
Ethylenediamine-tetraacetic acid extracted water-soluble matrix proteins in molluscan shells secreted from the mantle epithelia are believed to control crystal nucleation, morphology, orientation, and phase of the deposited mineral. Previously, atomic force microscopy demonstrated that abalone nacre proteins bind to growing step edges and to specific crystallographic faces of calcite, suggesting that inhibition of calcite growth may be one of the molecular processes required for growth of the… CONTINUE READING

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