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The 32 kDa Enamelin Undergoes Conformational Transitions upon Calcium Binding
The 32 kDa hydrophilic and acidic enamelin, the most stable cleavage fragment of the enamel specific glycoprotein, is believed to play vital roles in controlling crystal nucleation or growth during enamel biomineralization. Circular dichroism and Fourier transform infrared spectra demonstrate that t...
Tallennettuna:
| Päätekijät: | , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2008
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2574573/ https://ncbi.nlm.nih.gov/pubmed/18508280 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jsb.2008.04.007 |
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