The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution.

ABSTRACT: Amelogenin proteins are critical to the formation of enamel in teeth and may have roles in controlling growth and regulating microstructures of the intricately woven hydroxyapatite (HAP). Leucine-rich amelogenin protein (LRAP) is a 59-residue splice variant of amelogenin and contains the N- and C-terminal charged regions of the full-length protein thought to control crystal growth. Although the quaternary structure of full-length amelogenin in solution has been well studied and can consist of self-assemblies of monomers called nanospheres, there is limited information on the quaternary structure of LRAP. Here, sedimentation velocity analytical ultracentrifugation (SV) and small angle neutron scattering (SANS) were used to study the tertiary and quaternary structure of LRAP at various pH va

SUBMITTER: Tarasevich BJ 

PROVIDER: S-EPMC4400868 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature