id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-304254-67brxejx	Wei, Ping	The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase	2006-01-20		.txt	text/plain	4577	240	47	As we have reported previously, the peptide cleavage assay shows that the specific activity for proteolysis decreases linearly with the decrease of enzyme concentration, suggesting that the dimer is the major form for biological activity and that the dimeric interface could be targeted for structural-based drug design against SARS 3CL proteinase [18] . The crystal structure of SARS 3CL proteinase indicates that the N-finger fragment plays an important role in the dimerization and maintenance of the active form of the enzyme [16] . The dimer dissociation constants of the SARS 3CL proteinase and N-terminal mutants were determined by sedimentation velocity and equilibrium methods. In summary, we have carried out a mutational study on the N-finger of SARS 3CL proteinase and determined the dimer dissociation constants for the wild-type protein and the mutants using sedimentation velocity and equilibrium techniques.	./cache/cord-304254-67brxejx.txt	./txt/cord-304254-67brxejx.txt