id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-269756-tid8a464	Basso, Luis G. M.	SARS-CoV fusion peptides induce membrane surface ordering and curvature	2016-11-28		.txt	text/plain	12194	532	49	Although membrane fusion promoted by class I viral glycoproteins, such as SARS-CoV Spike, human immunodeficiency virus (HIV) gp160 or influenza virus hemagglutinin (HA), has been broadly studied in recent years [16] [17] [18] [19] , many aspects of the molecular mechanism behind the virus-host cell membrane fusion remain unknown, including conformational changes of the lipid bilayers during peptide-membrane interactions. In the present study, we investigated the effects of two putative fusion peptides from SARS-CoV S glycoprotein, corresponding to residues 770-788 (SARS FP ) and 873-888 (SARS IFP ) 13, 15, 22, 23 , on the structural dynamics, physicochemical properties, and thermotropic phase behavior of lipid model membranes by differential scanning calorimetry (DSC), continuous wave (CW) and pulsed electron spin resonance (ESR) along with nonlinear least-squares (NLLS) spectral fitting 24 .	./cache/cord-269756-tid8a464.txt	./txt/cord-269756-tid8a464.txt