Abstract
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 α-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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 162-167 |
| Number of pages | 6 |
| Journal | Journal of Magnetic Resonance |
| Volume | 144 |
| Issue number | 1 |
| DOIs | |
| State | Published - May 2000 |
Keywords
- Membrane proteins
- N solid-state NMR
- Orientational constraints
- Oriented samples
- PISEMA
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Nuclear and High Energy Physics
- Condensed Matter Physics
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Cite this
Wang, J., Denny, J., Tian, C., Kim, S., Mo, Y., Kovacs, F., Song, Z., Nishimura, K., Gan, Z., Fu, R., Quine, J. R., & Cross, T. A. (2000). Imaging Membrane Protein Helical Wheels. Journal of Magnetic Resonance, 144(1), 162-167. https://doi.org/10.1006/jmre.2000.2037