id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-291210-ghjseynl	Arbely, Eyal	A Highly Unusual Palindromic Transmembrane Helical Hairpin Formed by SARS Coronavirus E Protein	2004-08-13		.txt	text/plain	5568	320	55	2, 3 In an effort to better understand the components contributing to the pathogenic mechanism of the virus, we have structurally analyzed the transmembrane domain of SCoV E protein using Fourier Transform Infrared (FTIR) spectroscopy, X-ray scattering, electron microscopy and global searching molecular dynamics simulations. In order to examine the secondary structure of the transmembrane domain (TMD) of SCoV E protein, peptides were made which encompassed the entire hydrophobic region of the protein (Glu7-Arg38), as depicted in Figure 1 . So far three lines of evidence were obtained characterizing the transmembrane domain of SCoV E protein: (i) it is highly helical, (ii) it is composed of 26 amino acid residues and (iii) the helical elements are oriented normal to the membrane plane. As shown in Figure 4 , the electron density of lipid vesicles containing iodinated and unlabeled SCoV E protein transmembrane domain exhibit normal density profiles.	./cache/cord-291210-ghjseynl.txt	./txt/cord-291210-ghjseynl.txt