Structural Model of the Membrane-Bound C Terminus of Lipid-Modified Human N-Ras Protein (pages 5387–5390)
Guido Reuther, Kui-Thong Tan, Julia Köhler, Christine Nowak, André Pampel, Klaus Arnold, Jürgen Kuhlmann, Herbert Waldmann and Daniel Huster
Article first published online: 17 JUL 2006 | DOI: 10.1002/anie.200504266
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.