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- W2018557551 abstract "Surfaces of developing enamel crystals were shown to comprise of alternating domains of positive and less positive (perhaps even negative) charge density which directly bind a number of matrix proteins via electrostatic interactions. Studies using synthetic mineral crystals demonstrated stereo-specific docking of charged residues with crystal lattice sites. Preferential binding of matrix proteins to specific crystal faces related to interfacial hydrophobicity/hydrophobicity, was shown to control crystal habit." @default.
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- W2018557551 date "2002-03-01" @default.
- W2018557551 modified "2023-10-01" @default.
- W2018557551 title "Physico-chemical properties of crystal surfaces in matrix–mineral interactions during mammalian biomineralisation" @default.
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