id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-259416-gvzp2h5g	Ling, Shenglong	Combined approaches of EPR and NMR illustrate only one transmembrane helix in the human IFITM3	2016-04-05		.txt	text/plain	3975	228	50	Systematic site-directed spin labeling (SDSL) and electron paramagnetic resonance (EPR) studies of IFITM3 in detergent micelles identified a single, long transmembrane helix in the C-terminus and an intramembrane segment in the N-terminal hydrophobic region. Systematic site scanning of spin labeling, EPR dynamic and accessibility analysis identified a C-terminal transmembrane α -helix and an N-terminal IFITM3 segment (composed of two short α -helices) lying on the surface of micelles. Collectively, the analysis of the accessibility parameter (Π O2 and Π NiEDDA ) and the immersion depth parameter (Φ ) derived from the power saturation experiments demonstrated that the IFITM3 protein contains a long transmembrane α -helix covering the residue sequence from A96 to A131 in the putative hydrophobic region. Therefore, the combined EPR and solution NMR studies clearly supported the type II transmembrane protein topology model for IFITM3, which is consistent with the previously proposed mechanism of its antiviral function.	./cache/cord-259416-gvzp2h5g.txt	./txt/cord-259416-gvzp2h5g.txt