Imaging Membrane Protein Helical Wheels

J. Wang, J. Denny, C. Tian, S. Kim, Y. Mo, F. Kovacs, Z. Song, K. Nishimura, Z. Gan, R. Fu, J. R. Quine, T. A. Cross

Research output: Contribution to journalEditorialpeer-review

278 Scopus citations


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 languageEnglish (US)
Pages (from-to)162-167
Number of pages6
JournalJournal of Magnetic Resonance
Issue number1
StatePublished - May 2000
Externally publishedYes


  • Membrane proteins
  • N solid-state NMR
  • Orientational constraints
  • Oriented samples

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics


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