id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-356005-zhwtlik6	Yazhini, Arangasamy	D614G substitution enhances the stability of trimeric SARS-CoV-2 spike protein	2020-11-02		.txt	text/plain	2626	142	47	Here, using in-silico mutagenesis and energy calculations, we analyzed inter-residue interaction energies and thermodynamic stability of the dominant (G614) and the ancestral (D614) variants of spike protein trimer in 'closed' and 'partially open' conformations. Such changes in the local interaction energies enhance the thermodynamic stability of the spike protein trimer as free energy difference (ΔΔG) upon glycine substitution is −2.6 kcal/mol for closed conformation and −2.0 kcal/mol for open conformation. Our results on the structural and energetic basis of enhanced stability hint that G614 may confer increased availability of functional form of spike protein trimer and consequent in higher infectivity than the D614 variant. To study the effect of D614G variation on the thermodynamic stability of the spike protein trimer, we calculated free energy changes upon aspartate to glycine substitution using buildmodel function in FoldX (Schymkowitz et al., 2005) . The table contains details of frustration index of inter-residue contacts present at 614th position of spike protein trimer in closed and partially open conformations.	./cache/cord-356005-zhwtlik6.txt	./txt/cord-356005-zhwtlik6.txt