## Abstract The substrate‐like inhibition of serine proteinases by avian ovomucoid domains has provided an excellent model for protein inhibitor‐proteinase interactions of the standard type. ^1^H,^15^N and ^13^C NMR studies have been undertaken on complexes formed between turkey ovomucoid third dom
Effects of a structural change in collagen upon binding to conditioned dentin studied by13C NMR
✍ Scribed by Nishiyama, Norihiro ;Asakura, Tetsuo ;Suzuki, Kazuomi ;Horie, Kozo ;Nemoto, Kimiya
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 459 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0021-9304
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✦ Synopsis
To develop a better adhesive functional monomer, it is imperative to understand the adhesion mechanisms of the resin to the dentin surface. Bond strength to the decalcified dentin surface pretreated with dentin primer, an aqueous ethanol solution of N-methacryloyl glycine, increases by increasing the water content in the primer. The aqueous primer could increase the thickness of the hybrid layer. The structural change of dentinal collagen with NMaA was studied by using a model compound for collagen,-( 'Pro-2Pro-3Gly),o-, by I3C nuclear magnetic resonance (NMR). The model compound was aggregated in ethanol but dissociated in water. It was found that NMaA effectively dissociated the aggregated model compound in water. The dissociation of decalcified dentin was essential to create a thick hybrid layer that could afford a higher bond strength to dentin.
📜 SIMILAR VOLUMES
We have recorded high-resolution l3C-nmr spectra of collagen fibrils in the solid state by the cross-polarization-magic-angle-spinning (CP-MAS) method and analyzed the spectra with reference to those of collagenlike polypetides. We used two kinds of model polypeptides to obtain reference 13C chemica