High-resolution solid-state nuclear magnetic resonance spectra of dentin collagen.
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[1] Y. Kuboki,et al. Increase of dentin phosphophoryn with dentin formation. , 1988, Connective tissue research.
[2] J. T. Gerig,et al. Molecular dynamics of collagen side chains in hard and soft tissues. A multinuclear magnetic resonance study. , 1987, Biochemistry.
[3] W. Butler. Dentin-specific proteins. , 1987, Methods in enzymology.
[4] H. Saitô. Conformation‐dependent 13C chemical shifts: A new means of conformational characterization as obtained by high‐resolution solid‐state 13C NMR , 1986 .
[5] D. Torchia,et al. Nanosecond fluctuations of the molecular backbone of collagen in hard and soft tissues: a carbon-13 nuclear magnetic resonance relaxation study. , 1985, Biochemistry.
[6] H. Mook,et al. Neutron diffraction studies of collagen in fully mineralized bone. , 1985, Journal of molecular biology.
[7] H. Saito,et al. A high‐resolution 13C‐nmr study of collagenlike polypeptides and collagen fibrils in solid state studied by the cross‐polarization–magic angle‐spinning method. Manifestation of conformation‐dependent 13C chemical shifts and application to conformational characterization , 1984, Biopolymers.
[8] H. Saitǒ,et al. High-resolution carbon-13 NMR study of silk fibroin in the solid state by the cross-polarization-magic angle spinning method. Conformational characterization of silk I and silk II type forms of Bombyx mori fibroin by the conformation-dependent carbon-13 chemical shifts , 1984 .
[9] D. Torchia,et al. Solid state 13C NMR study of collagen molecular dynamics in hard and soft tissues. , 1983, The Journal of biological chemistry.
[10] E. J. Miller,et al. Preparation and characterization of the different types of collagen. , 1982, Methods in enzymology.
[11] M. Tsuzaki,et al. Location of the intermolecular cross-links in bovine dentin collagen, solubilization with trypsin and isolation of cross-link peptides containing dihydroxylysinonorleucine and pyridinoline. , 1981, Biochemical and biophysical research communications.
[12] Y. Kuboki,et al. Comparative collagen biochemistry of bovine periodontium, gingiva, and dental pulp. , 1981, Journal of dental research.
[13] Y. Kuboki,et al. Location of an intermolecular crosslink in bovine bone collagen. , 1981, Connective tissue research.
[14] Y. Kuboki,et al. Calcium-specific Precipitation of Dentin Phosphoprotein: A New Method of Purification and the Significance for the Mechanism of Calcification , 1979, Journal of dental research.
[15] A. Veis,et al. The Nature of Covalent Complexes of Phosphoproteins with Collagen in the Bovine Dentin Matrix , 1979, Journal of dental research.
[16] E. Stejskal,et al. Cross-polarization 13C nuclear magnetic resonance spectroscopy of collagen. , 1978, Archives of Biochemistry and Biophysics.
[17] D. Torchia,et al. 13C Magnetic resonance evidence for anisotropic molecular motion in collagen fibrils. , 1976, Journal of molecular biology.
[18] F. Gurd,et al. Carbon 13 nuclear magnetic resonance of pentapeptides of glycine containing central residues of methionine, proline, arginine, and lysine. , 1974, The Journal of biological chemistry.
[19] A. Veis,et al. THE MACROMOLECULAR ORGANIZATION OF DENTINE MATRIX COLLAGEN. I. CHARACTERIZATION OF DENTINE COLLAGEN. , 1964, Biochemistry.