id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-320175-w00rcvd8	Shi, Jiahai	The catalysis of the SARS 3C‐like protease is under extensive regulation by its extra domain	2006-02-08		.txt	text/plain	5485	261	51	Based on this, a super‐active triple‐mutant STI/A with a 3.7‐fold activity enhancement was thus engineered by mutating residues Ser284, Thr285 and Ile286 to Ala. The dynamic light scattering, CD and NMR characterizations indicate that the wild‐type (WT) and STI/A mutant share similar structural and dimerization properties, thus implying that in addition to dimerization, the extra domain might have other mechanisms to regulate the catalytic machinery. Based on this, a super-active triple-mutant STI ⁄ A with a 3.7-fold activity enhancement was thus engineered by mutating residues Ser284, Thr285 and Ile286 to Ala. The dynamic light scattering, CD and NMR characterizations indicate that the wild-type (WT) and STI ⁄ A mutant share similar structural and dimerization properties, thus implying that in addition to dimerization, the extra domain might have other mechanisms to regulate the catalytic machinery. Dynamic light scattering (DLS) was used to measure the apparent molecular mass resulting from monomer-dimer equilibrium of the wild-type and mutated proteases at three different NaCl concentrations.	./cache/cord-320175-w00rcvd8.txt	./txt/cord-320175-w00rcvd8.txt