title: Solid-state NMR analysis of crosslinking in mussel protein glue.
abstract: 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.
authors: Department of Chemistry, Washington University, St. Louis, Missouri 63130.
authors: S M
authors: SM
authors: Holl
authors: D
authors: D
authors: Hansen
authors: J H
authors: JH
authors: Waite
authors: J
authors: J
authors: Schaefer
mesh_terms: D000818:Animals; D049872:Bivalvia / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins; C037403:adhesive protein, mussel; D008239:Lysine