Enamel biomineralization: Solution- and solid-state NMR studies of a natural protein-mineral interface
EMSL Project ID
47735
Abstract
The protein amelogenin is the central protein that controls the formation of dental enamel, the hardest tissue in the human body. The protein orchestrates the nucleation, growth, and organization of enamel formation (amelogenesis) through the formation of large quaternary structures called nanospheres, consisting of 20-100 monomers. The structure and function of full-length amelogenin and LRAP, the latter a splice variant of amelogenin that contains only the charged N- and C- termini, are the focus of our four-year, NIH funded investigations. Solution-state structural studies are being conducted on full-length amelogen, two naturally occurring mutants, and LRAP, with an emphasis on characterizing structure under the variety of conditions found during enamel growth. Solid-state quantitative structural and orientation studies of the protein bound to hydroxyapatite are focused on LRAP, as its smaller size allows easy incorporation of selective isotopic labels which enable the determination of site specific, molecular level protein structure, protein-surface interactions and dynamics. Structural changes observed in solution or in the solid-state will then be correlated to differences in function.
Project Details
Start Date
2012-12-05
End Date
2013-11-13
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
A solution NMR investigation into the impaired self-assembly properties of two murine amelogenins containing the point mutations T21→I or P41→T
Buchko GW, G Lin, BJ Tarasevich, and WJ Shaw. 2013. "A solution NMR investigation into the impaired self-assembly properties of two murine amelogenins containing the point mutations T21?I or P41?T." Archives of Biochemistry and Biophysics 537(2):217-224. doi:10.1016/j.abb.2013.07.015