ArticleStructure (London, England : 1993)2010
Toward a structure determination method for biomineral-associated protein using combined solid- state NMR and computational structure prediction.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Solid-State NMR and MD Study of the Structure of the Statherin Mutant SNa15 on Mineral Surfaces.Journal of the American Chemical Society · 2019Article
- A REDOR ssNMR Investigation of the Role of an N-Terminus Lysine in R5 Silica Recognition.Langmuir : the ACS journal of surfaces and colloids · 2018Article
- Ubiquitin immobilized on mesoporous MCM41 silica surfaces - Analysis by solid-state NMR with biophysical and surface characterization.Biointerphases · 2017Article
- Core Amino Acid Residues in the Morphology-Regulating Protein, Mms6, for Intracellular Magnetite Biomineralization.Scientific reports · 2016Article
- Solid-state NMR studies of proteins immobilized on inorganic surfaces.Solid state nuclear magnetic resonance · 2015Review
- SFG analysis of surface bound proteins: a route towards structure determination.Physical chemistry chemical physics : PCCP · 2013Article
- Using the RosettaSurface algorithm to predict protein structure at mineral surfaces.Methods in enzymology · 2013Review
- Direct observation of phenylalanine orientations in statherin bound to hydroxyapatite surfaces.Journal of the American Chemical Society · 2012Article
- Computational reconstruction of multidomain proteins using atomic force microscopy data.Structure (London, England : 1993) · 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
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5 authors.
Funding
Abstract
Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. Unfortunately, the structure of biomineral-associated proteins cannot be determined by X-ray crystallography or solution nuclear magnetic resonance (NMR). Here we report a method for determining the structure of biomineral-associated proteins. The method combines solid-state NMR (ssNMR) and ssNMR-biased computational structure prediction. In addition, the algorithm is able to identify lattice geometries most compatible with ssNMR constraints, representing a quantitative, novel method for investigating crystal-face binding specificity. We use this method to determine most of the structure of human salivary statherin interacting with the mineral phase of tooth enamel. Computation and experiment converge on an ensemble of related structures and identify preferential binding at three crystal surfaces. The work represents a significant advance toward determining structure of biomineral-adsorbed protein using experimentally biased structure prediction. This method is generally applicable to proteins that can be chemically synthesized.
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