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