id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-301827-a7hnuxy5	Uversky, Vladimir N	A decade and a half of protein intrinsic disorder: Biology still waits for physics	2013-04-29		.txt	text/plain	20971	1059	43	94 Therefore, the abundance and peculiarities of the charged residues distribution within the protein sequences might determine physical and biological properties of extended IDPs and IDPRs. Also, simple polymer physics-based reasoning can give reasonably well-justified explanation of the conformational behavior of extended IDPs. In general, the conformational behavior of IDPs is characterized by the low cooperativity (or the complete lack thereof) of the denaturant-induced unfolding, lack of the measurable excess heat absorption peak(s) characteristic for the melting of ordered proteins, "turned out" response to heat and changes in pH, and the ability to gain structure in the presence of various binding partners. 183 This analysis revealed that proteins involved in regulation and execution of PCD possess substantial amount of intrinsic disorder and IDPRs were implemented in a number of crucial functions, such as protein-protein interactions, interactions with other partners including nucleic acids and other ligands, were shown to be enriched in post-translational modification sites, and were characterized by specific evolutionary patterns.	./cache/cord-301827-a7hnuxy5.txt	./txt/cord-301827-a7hnuxy5.txt