PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11857763-2	2002	In this study, we analyzed the effect of trifluoroethanol (TFE) on a myoglobin peptide and cytochrome c (cyt c) at low pH by circular dichroism (CD) and ESI-MS.	Trifluoroethanol	41-57	cytochrome c, somatic	Homo sapiens	91-103	
16322658-2	2005	We describe here the effect of trifluoroethanol (TFE) on cytochrome c equilibrium unfolding at different pH by nano-ESI-MS.	Trifluoroethanol	31-47	cytochrome c, somatic	Homo sapiens	57-69	
16322658-2	2005	We describe here the effect of trifluoroethanol (TFE) on cytochrome c equilibrium unfolding at different pH by nano-ESI-MS.	Trifluoroethanol	49-52	cytochrome c, somatic	Homo sapiens	57-69	
11857763-2	2002	In this study, we analyzed the effect of trifluoroethanol (TFE) on a myoglobin peptide and cytochrome c (cyt c) at low pH by circular dichroism (CD) and ESI-MS.	Trifluoroethanol	41-57	cytochrome c, somatic	Homo sapiens	105-110	
11857763-2	2002	In this study, we analyzed the effect of trifluoroethanol (TFE) on a myoglobin peptide and cytochrome c (cyt c) at low pH by circular dichroism (CD) and ESI-MS.	Trifluoroethanol	59-62	cytochrome c, somatic	Homo sapiens	91-103	
11857763-2	2002	In this study, we analyzed the effect of trifluoroethanol (TFE) on a myoglobin peptide and cytochrome c (cyt c) at low pH by circular dichroism (CD) and ESI-MS.	Trifluoroethanol	59-62	cytochrome c, somatic	Homo sapiens	105-110	
24729012-3	2014	A systemic investigation of polyethylene glycol (PEG) and trifluoroethanol (TFE) on the conformational stability of cyt c as a model hemeprotein was made using multi-methodological approach.	Trifluoroethanol	58-74	cytochrome c, somatic	Homo sapiens	116-121	
24729012-3	2014	A systemic investigation of polyethylene glycol (PEG) and trifluoroethanol (TFE) on the conformational stability of cyt c as a model hemeprotein was made using multi-methodological approach.	Trifluoroethanol	76-79	cytochrome c, somatic	Homo sapiens	116-121	
9675038-3	1998	Using both IR and CD spectroscopy, we demonstrate here that the TFE-induced nonnative alpha-helical structure in two beta-sheet-predominant proteins, beta-lactoglobulin and alpha-chymotrypsin, is unstable in comparison with those found in the alpha-helix-predominant proteins myoglobin and cytochrome c under identical conditions.	Trifluoroethanol	64-67	cytochrome c, somatic	Homo sapiens	290-302