Abstract
Solid-state NMR spectroscopy was used to determine a structural model of the backbone of the lipid anchor of membrane-bound N-Ras protein. The fully functional lipid-modified protein was obtained by ligating the expressed water-soluble N terminus with a chemically synthesized 13C-labeled lipidated peptide. After the NMR signals had been assigned by correlation experiments, a structural model was calculated from torsion angles derived from 1H and 13C chemical-shift data.
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