Summary
Structure and dynamics of a hydrophobic protein from bovine tooth enamel with a Mr ~19-20kD is derived from 2D NMR, Molecular mechanics-dynamics, and time-resolved picosecond fluorescence studies. Amelogenin is postulated to contain a hydrophobia core, β-spiral, encapsulated by a hydrophilic coat and seems to act as a Ca++ pump in the early stages of enamel mineralization.
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Renugopalakrishnan, V., Prabhakaran, M., Huang, SG., Cheung, H.C., Strawich, E., Glimcher, M.J. (1990). Structure and Dynamics of a ~19kD Phosphoprotein, Amelogenin, from Bovine Tooth Enamel. In: Vasilescu, D., Jaz, J., Packer, L., Pullman, B. (eds) Water and Ions in Biomolecular Systems. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7253-9_12
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DOI: https://doi.org/10.1007/978-3-0348-7253-9_12
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