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 journalEditorial

255 Scopus citations

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 languageEnglish (US)
Pages (from-to)162-167
Number of pages6
JournalJournal of Magnetic Resonance
Volume144
Issue number1
DOIs
StatePublished - 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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    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