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Biophys J, August 2000, p. 767-775, Vol. 79, No. 2
and¶
*National High Magnetic Field Laboratory, Institute
of Molecular Biophysics, ¶Department of Chemistry, and
Department of Mathematics, Florida State University,
Tallahassee, Florida 32306; and §Department of
Biochemistry and Cellular Biology, State University of New York, Stony
Brook, New York 11794 USA
The M2 protein from the influenza A virus forms a proton
channel in the virion that is essential for infection. This tetrameric protein appears to form a four-helix bundle spanning the viral membrane. Here the solid-state NMR method, 2D polarization inversion spin exchange at magic angle (PISEMA), has been used to obtain multiple
constraints from specifically amino acid-labeled samples. The
improvement of spectral resolution from 2D PISEMA over 1D methods and
2D separated local field methods is substantial. The reliability of the
method is validated by comparison of anisotropic chemical shift and
heteronuclear dipolar interactions from single site labeled samples.
The quantitative interpretation of the high-resolution constraints
confirms the helix tilt to be within the range of previous experimental
determinations (32°-38°). The binding of the channel inhibitor,
amantadine, results in no change in the backbone structure at position
Val27,28, which is thought to be a potential binding site
for the inhibitor.
Biophys J, August 2000, p. 767-775, Vol. 79, No. 2
© 2000 by the Biophysical Society 0006-3495/00/08/767/09 $2.00
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