id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-323871-2hx4fuk2	Ho, Sheau Ling	Structural bioinformatics analysis of free cysteines in protein environments	2009-03-14		.txt	text/plain	3244	198	59	For non-membrane proteins: the hydrophobic residues such as leucine, valine, isoleucine and alanine were more frequently seen in the spatial neighborhood around free cysteines; the same was observed for the aromatic phenylalanine residue. Thus, we applied a structure-base sequence alignment of these nine coronavirus main proteinases to identify any spatial correspondences involving cysteine among them. It can be observed that this multiple sequences alignment figure shows a strong conservation of hydrophobic residues (valine, leucine, isoleucine, alanine phenylalanine and proline) and small residues (serine and glycine) in proximity to cysteine residues. A superimposition (stereo image) of the structures of SARS 3CLpro demonstrates that cysteine residues not only favor positioning in a hydrophobic environment but also develop hunched posture in the surroundings of aromatic residues, see Fig. 3 .	./cache/cord-323871-2hx4fuk2.txt	./txt/cord-323871-2hx4fuk2.txt