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SARS Coronavirus E Protein in Phospholipid Bilayers: An X-Ray Study

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

^* Institute for X-ray Physics, University of Göttingen, Göttingen, Germany; Faculty of Science and Technology, Al-Quds University, Abu Dis, Jerusalem, Israel; and Alexander Silberman Institute of Life Sciences, Department of Biological Chemistry, The Hebrew University of Jerusalem, Givat-Ram, Jerusalem, Israel

Correspondence: Address reprint requests to T. Salditt, Institute for X-ray Physics, University of Göttingen, Friedrich-Hund-Platz 1, D-37077 Göttingen, Germany. Tel.: 49-551-399427; Fax: 49-551-399430; E-mail: tsaldit{at}gwdg.de.

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.

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