Structure determination of leucine-rich amelogenin protein adsorbed to hydroxyapatite using combined solid-state NMR and computational structure prediction
EMSL Project ID
38890
Abstract
The formation of biogenic materials requires the interaction of organic molecules with the mineral phase. In forming dental enamel, the mineralization of hydroxyapatite (HAp) is largely attributed to the protein amelogenin. Leucine-rich amelogenin protein (LRAP) is a naturally occurring splice variant of amelogenin, and comprises amelogenin's predicted HAp binding domains. We determined the structure of LRAP bound to HAp using combined solid-state NMR (ssNMR) and computational structure prediction. We generated initial structural models by biasing a structure-prediction algorithm (RosettaSurface) to satisfy all previously published ssNMR measurements (acquired from HAp-adsorbed LRAP). Initial structural models guided the placement of additional isotopic labels for a subsequent round of ssNMR measurements. Finally, we used the new and previously acquired ssNMR measurements to bias RosettaSurface structure prediction of HAp-adsorbed LRAP.
Project Details
Project type
Limited Scope
Start Date
2009-12-10
End Date
2010-01-07
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members