PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22813934-4	2012	Here, we used neutral detergents and anionic SDS to study the contribution of hydrophobic interactions to the folding of the CTD.	Sodium Dodecyl Sulfate	45-48	CTD	Homo sapiens	125-128	
22813934-9	2012	The greatest effect was observed in the fully phosphorylated CTD (three phosphate groups) in the presence of anionic SDS (7:1, detergent/CTD molar ratio); in these conditions, the CTD became an all-beta protein, with 83% beta-structure and no alpha-helix.	Sodium Dodecyl Sulfate	117-120	CTD	Homo sapiens	61-64	
22813934-9	2012	The greatest effect was observed in the fully phosphorylated CTD (three phosphate groups) in the presence of anionic SDS (7:1, detergent/CTD molar ratio); in these conditions, the CTD became an all-beta protein, with 83% beta-structure and no alpha-helix.	Sodium Dodecyl Sulfate	117-120	CTD	Homo sapiens	137-140	
22813934-9	2012	The greatest effect was observed in the fully phosphorylated CTD (three phosphate groups) in the presence of anionic SDS (7:1, detergent/CTD molar ratio); in these conditions, the CTD became an all-beta protein, with 83% beta-structure and no alpha-helix.	Sodium Dodecyl Sulfate	117-120	CTD	Homo sapiens	137-140