Abstract
Non-collagenous proteins such as osteocalcin function as regulators of the mineralization process in bone. Osteocalcin undergoes post-translational modification adding an extra carboxylate group on three of its glutamate residues to enhance interaction with bone mineral. In this work, we examine regulation of biomimetic apatite formation by osteocalcin that was not modified after translation. We analyze the structural features in the protein and mineral-protein interfaces to elicit the unmodified protein's fold inside the mineral and to unveil the species that interact with the mineral surface. The results presented here give clues on the protein's active role in controlling the mineral phases that are formed on hydroxyapatite crystals and its ability to influence the extent of order in these crystals.
Original language | English |
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Pages (from-to) | 104-114 |
Number of pages | 11 |
Journal | Journal of Structural Biology |
Volume | 207 |
Issue number | 2 |
DOIs | |
State | Published - 1 Aug 2019 |
Keywords
- Apatite regulation
- Biomineralization
- Mineral bound protein
- Non-collagenous proteins
- Protein conformation
- Protein-mineral interface
- Solid state NMR
All Science Journal Classification (ASJC) codes
- Structural Biology