Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and 13C–2H rotational-echo double-resonance solid-state NMR
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Residue-specific location of peptides in the hydrophobic core of membranes was examined using 13C–2H REDOR and samples in which the lipids were selectively deuterated. The transmembrane topology of the KALP peptide was validated with this approach with substantial dephasing observed for deuteration in the bilayer center and reduced or no dephasing for deuteration closer to the headgroups. Insertion of β sheet HIV and helical and β sheet influenza virus fusion peptides into the hydrophobic core of the membrane was validated in samples with extensively deuterated lipids.
KeywordsREDOR Membrane location Deuterated lipid Solid-state NMR Peptide Protein 13C–2H
The research was supported by NIH AI47153.
- de Planque MRR, Goormaghtigh E, Greathouse DV, Koeppe RE, Kruijtzer JAW, Liskamp RMJ, de Kruijff B, Killian JA (2001) Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation. Biochemistry 40:5000–5010CrossRefGoogle Scholar
- Qiang W, Bodner ML, Weliky DP (2008) Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries. J Am Chem Soc 130:5459–5471CrossRefGoogle Scholar
- Schmidt A, McKay RA, Schaefer J (1992) Internuclear distance measurement between deuterium (I = 1) and a spin-1/2 nucleus in rotating solids. J Magn Reson 96:644–650Google Scholar