id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-337681-579cz2tc	Sk, Md Fulbabu	Elucidating biophysical basis of binding of inhibitors to SARS-CoV-2 main protease by using molecular dynamics simulations and free energy calculations	2020-06-01		.txt	text/plain	5882	340	53	title: Elucidating biophysical basis of binding of inhibitors to SARS-CoV-2 main protease by using molecular dynamics simulations and free energy calculations In the present work, we have elucidated the mechanism of binding of two inhibitors, namely α-ketoamide and Z31792168, to SARS-CoV-2 main protease (M(pro) or 3CL(pro)) by using all-atom molecular dynamics simulations and free energy calculations. The initial coordinates for our molecular dynamics simulations were obtained from the X-ray crystallographic structure of the SARS-CoV-2 3CL pro complexed with the inhibitors a-ketoamide (PDB: 6Y2G) and Z31792168 (PDB: 5R84) (Berman et al., 2002; Zhang et al., 2020) . Next, in our study, the binding affinity of a-ketoamide was further evaluated and compared with the FDA approved anti-HIV protease inhibitors, such as lopinavir and darunavir, which has been reported as potent drugs against 3CL pro of SARS-CoV-2.	./cache/cord-337681-579cz2tc.txt	./txt/cord-337681-579cz2tc.txt