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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1993-5-12
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0003-9861
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
302
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
255-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1993
|
| pubmed:articleTitle |
Solid-state NMR analysis of crosslinking in mussel protein glue.
|
| pubmed:affiliation |
Department of Chemistry, Washington University, St. Louis, Missouri 63130.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|