Probing the self-association, intermolecular contacts, and folding propensity of amelogenin.

ABSTRACT: Amelogenins are an intrinsically disordered protein family that plays a major role in the development of tooth enamel, one of the most highly mineralized materials in nature. Monomeric porcine amelogenin possesses random coil and residual secondary structures, but it is not known which sequence regions would be conformationally attractive to potential enamel matrix targets such as other amelogenins (self-assembly), other matrix proteins, cell surfaces, or biominerals. To address this further, we investigated recombinant porcine amelogenin (rP172) using "solvent engineering" techniques to simultaneously promote native-like structure and induce amelogenin oligomerization in a manner that allows identification of intermolecular contacts between amelogenin molecules. We discovered that in the

SUBMITTER: Ndao M 

PROVIDER: S-EPMC3081550 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature