Imaging membrane protein helical wheels.
Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this alpha-helix. The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid specific labels around the "PISA wheel" defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained.
Wang
J
J
National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, USA.
Denny
J
J
Tian
C
C
Kim
S
S
Mo
Y
Y
Kovacs
F
F
Song
Z
Z
Nishimura
K
K
Gan
Z
Z
Fu
R
R
Quine
J R
JR
Cross
T A
TA
D009980:Influenza A virus; D008051:Lipid Bilayers / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary
D008051:Lipid Bilayers; D008565:Membrane Proteins; D009587:Nitrogen Isotopes