id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-342639-vf9n2vf9	Chang, Chung-ke	Transient Oligomerization of the SARS-CoV N Protein – Implication for Virus Ribonucleoprotein Packaging	2013-05-23		.txt	text/plain	5386	243	42	For disulfide trapping experiments, we chose mutation sites that would form disulfide linkages based on the crystal packing structures of the SARS-CoV N protein CTD ( Figure 1 ) [9] . Within the crystal asymmetric unit, the SARS-CoV N protein CTD packs as an octamer which stacks to form a helical arrangement with a continuous positively charged surface that could potentially allow the RNA to bind to it through electrostatic interactions ( Fig. 1 ) [9] . By disulfide trapping technique we measured the amount of transient oligomers of N protein mutants with strategically located cysteine residues and showed that SARS-CoV N protein is capable of transient oligomerization in solution through the CTD in the absence of nucleic acids. Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA	./cache/cord-342639-vf9n2vf9.txt	./txt/cord-342639-vf9n2vf9.txt