id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-326441-w8iyh59u	Bhattacharjee, Sayan	Transmission of allosteric response within the homotrimer of SARS-CoV-2 spike upon recognition of ACE2 receptor by the receptor-binding domain	2020-09-06		.txt	text/plain	2426	129	48	The pathogenesis of novel SARS-CoV-2 virus initiates through recognition of ACE2 receptor (Angiotensin-converting enzyme 2) of the host cells by the receptor-binding domain (RBD) located at spikes of the virus. Using MD simulations, we have demonstrated allosteric crosstalk within RBD in apoand receptor-bound states where dynamic correlated motions and electrostatic energy perturbations contribute. To probe deeper into the dynamicity of free and ACE2-bound RBD of the COVID spike protein, Cα atoms based root mean square fluctuations (RMSF) and Order parameter (S 2 ) considering the N-H vectors 9 of RBD, were calculated from the corresponding trajectories. The residue wise non-bonded interaction energy between free RBD and its bound state with ACE2 was described as: Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor	./cache/cord-326441-w8iyh59u.txt	./txt/cord-326441-w8iyh59u.txt