id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-290446-43h1r4pm	Vazquez, Leonardo	Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus	2017-07-27		.txt	text/plain	8840	422	53	This spacer provided a reasonably dynamic loop, according to our NMR data, which included narrow chemical shift dispersion (S2A Fig As depicted in Fig 1A, we designed the nsp1 constructs so as to avoid truncating their secondary-structure elements. The full-length nsp1 fusion protein has only a few missing peaks, indicating a well-folded 3D domain, which causes a wide dispersion of chemical shifts and allows straightforward identification of backbone HN signals. The SSP indicates the propensity ranging from -1 to 1 to adopt backbone conformations typical for extended β-strands or helical structures, respectively, according to the effect of these conformations on the chemical shifts of backbone atoms, [39] [40] [41] As shown in Fig 7, with the SSP algorithm it was possible to define very well the secondarystructure elements of the folded globular domain of nsp1 (orange bars in the uppermost graph).	./cache/cord-290446-43h1r4pm.txt	./txt/cord-290446-43h1r4pm.txt