Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.

Journal article

We report the first example of 17O NMR spectra from a selectively labeled transmembrane peptide, 17O-[Ala12]-WALP23, as a lyophilized powder and incorporated in hydrated phospholipid vesicles. It is shown that at high magnetic field it is feasible to apply 17O NMR to the study of membrane-incorporated peptides. Furthermore, we were able to estimate distances within the selectively labeled WALP peptide, which represents a consensus transmembrane protein sequence. This work opens up new applications of 17O solid-state NMR on biological systems.

Authors: Lemaître, V; de Planque, MR; Howes, A; Smith, M; Dupree, R

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 126
• Issue: 47
• Pages: 15320-15321
• Publication date: 2004-12-01
• DOI: 10.1021/ja0473283
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Nuclear Magnetic Resonance, Biomolecular; Cell Membrane; Peptides; Membrane Proteins; Models, Molecular; Oxygen Isotopes