Use of isotope-edited FTIR to derive a backbone structure of a transmembrane protein

Joshua Manor, Eyal Arbely, Andrè Beerlink, Mutaz Akkawi, Isaiah T. Arkin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Solving structures of membrane proteins has always been a formidable challenge, yet even upon success, the results are normally obtained in a mimetic environment that can be substantially different from a biological membrane. Herein, we use noninvasive isotope-edited FTIR spectroscopy to derive a structural model for the SARS coronavirus E protein transmembrane domain in lipid bilayers. Molecular-dynamics-based structural refinement, incorporating the IR-derived orientational restraints points to the formation of a helical hairpin structure. Disulfide cross-linking and X-ray reflectivity depth profiling provide independent support of the results. The unusually short helical hairpin structure of the protein might explain its ability to deform bilayers and is reminiscent of other peptides with membrane disrupting functionalities. Taken together, we show that isotope-edited FTIR is a powerful tool to analyze small membrane proteins in their native environment, enabling us to relate the unusual structure of the SARS E protein to its function.

Original languageAmerican English
Pages (from-to)2573-2579
Number of pages7
JournalJournal of Physical Chemistry Letters
Issue number15
StatePublished - 7 Aug 2014


  • E protein
  • SARS coronavirus
  • dichroism
  • orientational constraint
  • protein refinement


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