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Default Solid-state NMR analysis of crosslinking in mussel protein glue.

Solid-state NMR analysis of crosslinking in mussel protein glue.

Related Articles Solid-state NMR analysis of crosslinking in mussel protein glue.

Arch Biochem Biophys. 1993 Apr;302(1):255-8

Authors: Holl SM, Hansen D, Waite JH, Schaefer J

Solid-state 13C and 15N NMR spectra have been obtained of intact adhesive plaques from the mussel Geukensia demissa labeled by L-[6-13C,6-15N]lysine. The plaques are rich in a polyphenolic protein glue which has 50 or more repeats of a nonapeptide sequence with one lysine per repeat. The average isotopic 15N enrichment of lysyl epsilon nitrogens in the plaques was 4%. These lysyl amines are not involved in ionic complexes and do not form observable concentrations of covalent crosslinks.

PMID: 8470902 [PubMed - indexed for MEDLINE]



Source: PubMed
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