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A simple but efficient (13)C MAS NMR method is presented for the determination of the location of embedded molecules such as peptides relative to biological membrane surfaces by exploiting the interaction with paramagnetic lanthanide ions. Using various aqueous Dy(3+) concentrations a distance-dependent differential paramagnetic quenching of NMR lipid resonance intensities for specific carbon sites was observed, with residues at the bilayer surface quenched effectively and hydrophobic sites unaffected by Dy(3+). Tested on the membrane-embedded 50 residue long M13 coat protein, (13)C labeled at its Val-29 and Val-31 residues, no paramagnetic quenching was observed for the peptide resonances by Dy(3+), suggesting that Val-29 and Val-31 are not in close proximity to the bilayer interface, but buried deeply inside the hydrophobic region of the lipid bilayer.

Original publication

DOI

10.1006/jmre.1999.1894

Type

Journal article

Journal

J Magn Reson

Publication Date

12/1999

Volume

141

Pages

335 - 339

Keywords

Carbon Isotopes, Dimyristoylphosphatidylcholine, Indicators and Reagents, Lipid Bilayers, Membrane Proteins, Metals, Rare Earth, Molecular Conformation, Nuclear Magnetic Resonance, Biomolecular, Peptides