PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12360528-0	2002	Molten globule of bovine alpha-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis.	Trifluoroethanol	74-90	lactalbumin alpha	Bos taurus	25-42	
17786546-1	2007	A mixture of 4-chloro-1-butanol and 2,2,2-Trifluoroethanol (TFE) has been used to generate Molten globule (MG) state of structurally homologous but functionally different proteins bovine alpha-lactalbumin and hen egg-white lysozyme.	Trifluoroethanol	36-58	lactalbumin alpha	Bos taurus	187-204	
17786546-1	2007	A mixture of 4-chloro-1-butanol and 2,2,2-Trifluoroethanol (TFE) has been used to generate Molten globule (MG) state of structurally homologous but functionally different proteins bovine alpha-lactalbumin and hen egg-white lysozyme.	Trifluoroethanol	60-63	lactalbumin alpha	Bos taurus	187-204	
11488928-2	2001	Bovine alpha-lactalbumin (alpha-LA) is an alpha/beta protein which adopts partly folded states when dissolved at low pH (A-state), by removal of the protein-bound calcium at neutral pH and low salt concentration (apo-state), as well as in aqueous trifluoroethanol.	Trifluoroethanol	247-263	lactalbumin alpha	Bos taurus	7-24	
11488928-2	2001	Bovine alpha-lactalbumin (alpha-LA) is an alpha/beta protein which adopts partly folded states when dissolved at low pH (A-state), by removal of the protein-bound calcium at neutral pH and low salt concentration (apo-state), as well as in aqueous trifluoroethanol.	Trifluoroethanol	247-263	lactalbumin alpha	Bos taurus	26-34	
11488928-6	2001	A nicked alpha-LA species consisting of fragments 1-,3-40 and 41-123 (nicked-LA) was prepared by thermolytic digestion of the 123-residue chain of alpha-LA in 50% (v/v) aqueous trifluoroethanol.	Trifluoroethanol	177-193	lactalbumin alpha	Bos taurus	9-17	
11451435-0	2001	Trifluoroethanol-assisted protein folding: fragment 53--103 of bovine alpha-lactalbumin.	Trifluoroethanol	0-16	lactalbumin alpha	Bos taurus	70-87	
10091665-0	1999	Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A.	Trifluoroethanol	0-16	lactalbumin alpha	Bos taurus	110-127	
10091665-1	1999	The trifluoroethanol (TFE)-induced structural changes of two proteins widely used in folding experiments, bovine alpha-lactalbumin, and bovine pancreatic ribonuclease A, have been investigated.	Trifluoroethanol	4-20	lactalbumin alpha	Bos taurus	113-130	
10091665-1	1999	The trifluoroethanol (TFE)-induced structural changes of two proteins widely used in folding experiments, bovine alpha-lactalbumin, and bovine pancreatic ribonuclease A, have been investigated.	Trifluoroethanol	22-25	lactalbumin alpha	Bos taurus	113-130	
10091665-3	1999	Both proteins behave rather differently under the influence of TFE: alpha-lactalbumin exhibits a molten globule state at low TFE concentrations before it reaches the so-called TFE state, whereas ribonuclease A is directly transformed into the TFE state at TFE concentrations above 40% (v/v).	Trifluoroethanol	63-66	lactalbumin alpha	Bos taurus	68-85	
10091665-3	1999	Both proteins behave rather differently under the influence of TFE: alpha-lactalbumin exhibits a molten globule state at low TFE concentrations before it reaches the so-called TFE state, whereas ribonuclease A is directly transformed into the TFE state at TFE concentrations above 40% (v/v).	Trifluoroethanol	125-128	lactalbumin alpha	Bos taurus	68-85	
10091665-3	1999	Both proteins behave rather differently under the influence of TFE: alpha-lactalbumin exhibits a molten globule state at low TFE concentrations before it reaches the so-called TFE state, whereas ribonuclease A is directly transformed into the TFE state at TFE concentrations above 40% (v/v).	Trifluoroethanol	125-128	lactalbumin alpha	Bos taurus	68-85	
10091665-3	1999	Both proteins behave rather differently under the influence of TFE: alpha-lactalbumin exhibits a molten globule state at low TFE concentrations before it reaches the so-called TFE state, whereas ribonuclease A is directly transformed into the TFE state at TFE concentrations above 40% (v/v).	Trifluoroethanol	125-128	lactalbumin alpha	Bos taurus	68-85	
10091665-3	1999	Both proteins behave rather differently under the influence of TFE: alpha-lactalbumin exhibits a molten globule state at low TFE concentrations before it reaches the so-called TFE state, whereas ribonuclease A is directly transformed into the TFE state at TFE concentrations above 40% (v/v).	Trifluoroethanol	125-128	lactalbumin alpha	Bos taurus	68-85	
8289283-0	1994	Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin.	Trifluoroethanol	22-38	lactalbumin alpha	Bos taurus	73-90	
8289283-9	1994	The line narrowing observed in the TFE state has made it possible to obtain directly sequence-specific assignments for about 25% of the 123 residues of bovine alpha-lactalbumin in 50% (v/v) TFE.	Trifluoroethanol	35-38	lactalbumin alpha	Bos taurus	159-176	
8289283-9	1994	The line narrowing observed in the TFE state has made it possible to obtain directly sequence-specific assignments for about 25% of the 123 residues of bovine alpha-lactalbumin in 50% (v/v) TFE.	Trifluoroethanol	190-193	lactalbumin alpha	Bos taurus	159-176