The molecular structure of the neutral-soluble proteins of embryonic bovine enamel in the solid state.

@article{Bonar1965TheMS,
  title={The molecular structure of the neutral-soluble proteins of embryonic bovine enamel in the solid state.},
  author={Laurence C. Bonar and Melvin J. Glimcher and Gerald L. Mechanic},
  journal={Journal of ultrastructure research},
  year={1965},
  volume={13 3},
  pages={
          308-17
        }
}
Cross-β X-ray diffraction patterns have been obtained from fibers prepared from the cold, neutral-soluble protein fraction of decalcified, bovine, embryonic enamel matrix. Similar cross-β patterns have previously been reported from the intact organic matrix (8). The structural implications of the unusually high proline content of these proteins are discussed. 

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