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Biophys J, July 2002, p. 345-358, Vol. 83, No. 1
and
*Department of Biochemistry, University of Western Ontario, London
N6A 5C1, Canada; and Department of Physics, Memorial
University of Newfoundland, St. John's, Newfoundland A1B 3X7, Canada
Selectively deuterated transmembrane peptides comprising
alternating leucine-alanine subunits were examined in fluid bilayer membranes by solid-state nuclear magnetic resonance (NMR) spectroscopy in an effort to gain insight into the behavior of membrane proteins. Two groups of peptides were studied: 21-mers having a 17-amino-acid hydrophobic domain calculated to be close in length to the hydrophobic thickness of 1-palmitoyl-2-oleoyl phosphatidylcholine and 26-mers having a 22-amino-acid hydrophobic domain calculated to exceed the
membrane hydrophobic thickness. 2H NMR spectral features
similar to ones observed for transmembrane peptides from single-span
receptors of higher animal cells were identified which apparently
correspond to effectively monomeric peptide. Spectral observations
suggested significant distortion of the transmembrane 
-helix, and/or
potential for restriction of rotation about the tilted helix long axis
for even simple peptides. Quadrupole splittings arising from the 26-mer
were consistent with greater peptide "tilt" than were those of the
analogous 21-mer. Quadrupole splittings associated with monomeric
peptide were relatively insensitive to concentration and temperature
over the range studied, indicating stable average conformations, and a
well-ordered rotation axis. At high peptide concentration (6 mol%
relative to phospholipid) it appeared that the peptide predicted to be
longer than the membrane thickness had a particular tendency toward
reversible peptide-peptide interactions occurring on a timescale
comparable with or faster than ~10
5 s. This interaction
may be direct or lipid-mediated and was manifest as line broadening.
Peptide rotational diffusion rates within the membrane, calculated from
quadrupolar relaxation times, T2e, were
consistent with such interactions. In the case of the peptide predicted
to be equal to the membrane thickness, at low peptide concentration
spectral lineshape indicated the additional presence of a population of
peptide having rotational motion that was restricted on a timescale of
105 s.
Biophys J, July 2002, p. 345-358, Vol. 83, No. 1
© 2002 by the Biophysical Society 0006-3495/02/07/345/14 $2.00
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