id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-310062-mmlh9i1o	Luo, Haibin	In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS	2004-12-01		.txt	text/plain	5161	269	54	Both the thermal and chemical denaturant-induced denaturation analyses showed that oligomeric SARS_NP unfolds and refolds through a two-state model, and the electrostatic interactions among the charge groups of SARS_NP made a significant contribution to its conformational stability. In addition, the unfolding and refolding characterizations of SARS _ NP dimer caused by thermaland chemical denaturant-induced denaturations were also inspected by fluorescent and CD spectral investigation, it is found that SARS _ NP exhibits its most stable conformation near pH 9.0, and its oligomer dissociation and protein unfolding seem to be of coinstantaneous occurring events. The fluorescent intensity was found to decrease with increase of temperature accompanied by a shift in emission k max from 333 to 343 nm ( Fig. 4A and C) , whereas far-UV CD spectral information suggested the loss of secondary structure for SARS _ NP during its thermal-induced denaturation (Fig. 4B and D) .	./cache/cord-310062-mmlh9i1o.txt	./txt/cord-310062-mmlh9i1o.txt