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Updated: Jul 10, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes
Vincent Lemaître1, Maurits R R de Planque, Andy P Howes
1BioAnalytical Department Vers-Chez-Les-Blanc, Nestlé Research Center, CH-1000 Lausanne 26, Switzerland.
Abstract:
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.
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