Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite.

ABSTRACT: Biomineralization processes govern the formation of hierarchical hard tissues such as bone and teeth in living organisms, and mimicking these processes could lead to the design of new materials with specialized properties. However, such advances require structural characterization of the proteins guiding biomineral formation to understand and mimic their impact. In their "active" form, biomineralization proteins are bound to a solid surface, severely limiting our ability to use many conventional structure characterization techniques. Here, solid-state NMR spectroscopy was applied to study the intermolecular interactions of amelogenin, the most abundant protein present during the early stages of enamel formation, in self-assembled oligomers bound to hydroxyapatite. Intermolecular dipolar co

SUBMITTER: Arachchige RJ 

PROVIDER: S-EPMC6225022 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature