SARS Coronavirus E protein in phospholipid bilayers: An X-ray study

Z. Khattari, G. Brotons, M. Akkawi, E. Arbely, I. T. Arkin, T. Salditt*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


We investigated the structure of the hydrophobic domain of the severe acute respiratory syndrome E protein in model lipid membranes by x-ray reflectivity and x-ray scattering. In particular, we used x-ray reflectivity to study the location of an iodine-labeled residue within the lipid bilayer. The label imposes spatial constraints on the protein topology. Experimental data taken as a function of protein/lipid ratio P/L and different swelling states support the hairpin conformation of severe acute respiratory syndrome E protein reported previously. Changes in the bilayer thickness and acyl-chain ordering are presented as a function of P/L, and discussed in view of different structural models.

Original languageAmerican English
Pages (from-to)2038-2050
Number of pages13
JournalBiophysical Journal
Issue number6
StatePublished - Mar 2006

Bibliographical note

Funding Information:
We gratefully acknowledge financial support from the Deutsche Forschungsgemeinschaft through the German-Israel-Palestine trilateral project SA 7772/6-1.


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