ArticleBiophysical journal2009
Solution- and adsorbed-state structural ensembles predicted for the statherin-hydroxyapatite system.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 56 citations in OpenAlex.
- Biomedical applications of solid-binding peptides and proteins.Materials today. Bio · 2023Review
- Harnessing biomolecules for bioinspired dental biomaterials.Journal of materials chemistry. B · 2020Review
- Cell and Material-Specific Phage Display Peptides Increase iPS-MSC Mediated Bone and Vasculature Formation In Vivo.Advanced healthcare materials · 2019Article
- Solid-State NMR and MD Study of the Structure of the Statherin Mutant SNa15 on Mineral Surfaces.Journal of the American Chemical Society · 2019Article
- Solid-state NMR studies of proteins immobilized on inorganic surfaces.Solid state nuclear magnetic resonance · 2015Review
- Neutron reflectometry studies of the adsorbed structure of the amelogenin, LRAP.The journal of physical chemistry. B · 2013Article
- Using the RosettaSurface algorithm to predict protein structure at mineral surfaces.Methods in enzymology · 2013Review
- Cementomimetics-constructing a cementum-like biomineralized microlayer via amelogenin-derived peptides.International journal of oral science · 2012Article
- Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite.The journal of physical chemistry. C, Nanomaterials and interfaces · 2011Article
- Toward a structure determination method for biomineral-associated protein using combined solid- state NMR and computational structure prediction.Structure (London, England : 1993) · 2010Article
- Phosphorylation-dependent mineral-type specificity for apatite-binding peptide sequences.Biomaterials · 2010Article
- The Role of Basic Amino Acids in the Molecular Recognition of Hydroxyapatite by Statherin using Solid State NMR.Surface science · 2010Article
- Sum frequency generation and solid-state NMR study of the structure, orientation, and dynamics of polystyrene-adsorbed peptides.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Article
- Exploiting fluorescence resonance energy transfer to probe structural changes in a macromolecule during adsorption and incorporation into a growing biomineral crystal.Colloids and surfaces. B, Biointerfaces · 2009Article
- Modulation of calcium oxalate dihydrate growth by selective crystal-face binding of phosphorylated osteopontin and polyaspartate peptide showing occlusion by sectoral (compositional) zoning.The Journal of biological chemistry · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We have developed a multiscale structure prediction technique to study solution- and adsorbed-state ensembles of biomineralization proteins. The algorithm employs a Metropolis Monte Carlo-plus-minimization strategy that varies all torsional and rigid-body protein degrees of freedom. We applied the technique to fold statherin, starting from a fully extended peptide chain in solution, in the presence of hydroxyapatite (HAp) (001), (010), and (100) monoclinic crystals. Blind (unbiased) predictions capture experimentally observed macroscopic and high-resolution structural features and show minimal statherin structural change upon adsorption. The dominant structural difference between solution and adsorbed states is an experimentally observed folding event in statherin's helical binding domain. Whereas predicted statherin conformers vary slightly at three different HAp crystal faces, geometric and chemical similarities of the surfaces allow structurally promiscuous binding. Finally, we compare blind predictions with those obtained from simulation biased to satisfy all previously published solid-state NMR (ssNMR) distance and angle measurements (acquired from HAp-adsorbed statherin). Atomic clashes in these structures suggest a plausible, alternative interpretation of some ssNMR measurements as intermolecular rather than intramolecular. This work demonstrates that a combination of ssNMR and structure prediction could effectively determine high-resolution protein structures at biomineral interfaces.
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