id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-314329-rzda8x62	Wells, Stephen A.	Rigidity, normal modes and flexible motion of a SARS-CoV-2 (COVID-19) protease structure	2020-03-12		.txt	text/plain	4108	208	50	A judicious combination of simplified methodologiesrigidity analysis, elastic network modelling, and geometric simulation of flexible motioncan work together to extract valuable information on the large-amplitude, low-frequency motions of a protein structure, at a fraction of the computational cost (in resources and time) of molecular dynamics (MD) approaches [3] . The simulations reported here suggest that the protease structure is capable of substantial flexible motions which alter domain orientations, open and close clefts, and affect the geometry of an inhibitor-binding site. The rigidity and flexibility of two recently reported crystal structures (PDB entries 6Y2E and 6LU7) of a protease from the SARS-CoV-2 virus, the infectious agent of the COVID-19 respiratory disease, has been investigated using pebble-game rigidity analysis, elastic network model normal mode analysis, and all-atom geometric simulations. The rigidity and flexibility of two recently reported crystal structures (PDB entries 6Y2E and 6LU7) of a protease from the SARS-CoV-2 virus, the infectious agent of the COVID-19 respiratory disease, has been investigated using pebble-game rigidity analysis, elastic network model normal mode analysis, and all-atom geometric simulations.	./cache/cord-314329-rzda8x62.txt	./txt/cord-314329-rzda8x62.txt