id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-314746-1o0rf0ii	Bergasa-Caceres, Fernando	Interdiction of Protein Folding for Therapeutic Drug Development in SARS CoV-2	2020-08-10		.txt	text/plain	5038	304	56	[Image: see text] In this article, we predict the folding initiation events of the ribose phosphatase domain of protein Nsp3 and the receptor binding domain of the spike protein from the severe acute respiratory syndrome (SARS) coronavirus-2. The identification of the primary contacts along the folding pathway of viral proteins constitutes an important result for at least two reasons: (a) the sequences of the specific segments involved in the primary contacts provide a template to specify candidate peptide drugs of inhibitory effect with the maximum possible contact affinity to compete with the natural folding mechanism; and (b) it provides insight for further investigation into the subsequent folding steps leading to a fully functional viral protein, potentially providing for additional FITRs. The fact that the primary contact is defined by the interaction between two well defined amino acid sequences suggests that a strategy to develop FITR-based therapeutic drugs could be one utilizing trial peptide drugs as suggested above.	./cache/cord-314746-1o0rf0ii.txt	./txt/cord-314746-1o0rf0ii.txt