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. 1990 Mar 16;167(2):761-6.
doi: 10.1016/0006-291x(90)92090-m.

High-resolution solid-state nuclear magnetic resonance spectra of dentin collagen

R Fujisawa  1 , Y Kuboki
Affiliations

High-resolution solid-state nuclear magnetic resonance spectra of dentin collagen

R Fujisawa et al. Biochem Biophys Res Commun. .

Abstract

Insoluble collagen of bovine dentin was characterized by high-resolution solid-state 13C nuclear magnetic resonance (NMR) spectroscopy using a cross-polarization magic angle spinning procedure. A downfield shift was observed in the signal of hydroxyproline C beta compared with that in skin collagen, indicating a distortion in the hydroxyproline structure. A signal of 31P NMR was detected in dentin collagen that was compatible with the presence of matrix-associated phosphoprotein.

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