PNNL-USC team discovers how protein in teeth controls bone-like crystals to form steely enamel
Sculpting Enamel From Bone: Top right: an electron microscope captures the weave structure of the long crystal stands that give enamel its strength. Bottom: A model based on nuclear magnetic resonance data derived at Pacific Northwest National Laboratory that shows how an active portion of the enamel-building protein, an amelogenin called LRAP, interacts with the crystal hydroxyapatite, or HAP, used by the body to engineer both bone and enamel. An isotopically labeled amino acid group (yellow, just left of center) in LRAP is near the HAP surface, a closeness that appears to encourage full interaction of protein with HAP that enables the protein to dictate the pattern of crystal formation.
Bone and enamel start with the same calcium-phosphate crystal building material but end up quite different in structure and physical properties. The difference in bone and enamel microstructure is attributed to a key protein in enamel that molds crystals into strands thousands of times longer and much stronger than those in bone. The dimension of an enamel strand is 100,000 by 50 by 25 nanometers; bone is 35 by 25 by 4 nanometers.
But how that protein achieves this feat of crystal-strand shape-shifting has remained elusive. Today, scientists have reported the first direct observation of how this protein, amelogenin, interacts with crystals like those in bone to form the hard, protective enamel of teeth.
Bill Cannon | EurekAlert!
The “TRiC” to folding actin
10.08.2018 | Max-Planck-Institut für Biochemie
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10.08.2018 | Institute of Physical Chemistry of the Polish Academy of Sciences
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