Investigation of the Nature of the Protein−Mineral Interface in Bone by Solid-State NMR
- 20 May 2005
- journal article
- research article
- Published by American Chemical Society (ACS) in Chemistry of Materials
- Vol. 17 (12) , 3059-3061
- https://doi.org/10.1021/cm050492k
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Bone recognition mechanism of porcine osteocalcin from crystal structureNature, 2003
- Structural Studies of Biomaterials Using Double-Quantum Solid-State NMR SpectroscopyAnnual Review of Physical Chemistry, 2003
- SPARC, a matricellular protein: at the crossroads of cell–matrixMatrix Biology, 2000
- THE MATERIAL BONE: Structure-Mechanical Function RelationsAnnual Review of Materials Science, 1998
- COLLAGENS: Molecular Biology, Diseases, and Potentials for TherapyAnnual Review of Biochemistry, 1995
- The strength of a calcified tissue depends in part on the molecular structure and organization of its constituent mineral crystals in their organic matrixBone, 1995
- The carbonate environment in bone mineral: A resolution-enhanced fourier transform infrared spectroscopy studyCalcified Tissue International, 1989
- The geometry of calcium carboxylate interactions in crystalline complexesActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1981
- Direct identification of the calcium-binding amino acid, gamma-carboxyglutamate, in mineralized tissue.Proceedings of the National Academy of Sciences, 1975
- Molecular structures of amino acids and peptides. II. A redetermination of the crystal structure of L-O-serine phosphate. A very short phosphate–carboxyl hydrogen bondActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1970