期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 132, 期 45, 页码 16052-16057出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja104827k
关键词
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资金
- National Science Foundation [MCB-0613019]
- Burroughs Wellcome Fund
We present a new method that integrates selective biosynthetic labeling and solid-state NMR detection to identify in situ important protein cross-links in plant cell walls. We have labeled soybean cells by growth in media containing L-[ring-d(4)]tyrosine and L-[ring-4-(13)C]tyrosine, compared whole-cell and cell-wall (13)C CPMAS spectra, and examined intact cell walls using (13)C{(2)H} rotational echo double-resonance (REDOR) solid-state NMR. The proximity of (13)C and (2)H labels shows that 25% of the tyrosines in soybean cell walls are part of isodityrosine cross-links between protein chains. We also used (15)N{(13)C) REDOR of intact cell walls labeled by L-[epsilon-(15)N,6-(13)C]lysine and depleted in natural-abundance (15)N to establish that the side chains of lysine are not significantly involved in covalent cross-links to proteins or sugars.
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