Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
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.
Lemaître
Vincent
V
BioAnalytical Department Vers-Chez-Les-Blanc, Nestlé Research Center, CH-1000 Lausanne 26, Switzerland.
de Planque
Maurits R R
MR
Howes
Andy P
AP
Smith
Mark E
ME
Dupree
Ray
R
Watts
Anthony
A
D002462:Cell Membrane / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010103:Oxygen Isotopes; D010455:Peptides / Q000737:chemistry*
D008565:Membrane Proteins; D010103:Oxygen Isotopes; D010455:Peptides