PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2406266-9	1990	CD studies provided evidence that histatin 5 and the longer fragments, C16, N16, and C14 preferred alpha-helical conformations in non-aqueous solvents such as trifluoroethanol and methanol, while in water and pH 7.4 phosphate buffers, they favored random coil structures.	Trifluoroethanol	159-175	histatin 3	Homo sapiens	34-44	
9923693-2	1998	Histatin 5 has no defined structure in H2O but adopts a more helical conformation in dimethyl sulfoxide and aqueous trifluoroethanol.	Trifluoroethanol	116-132	histatin 3	Homo sapiens	0-10	
11454169-0	2001	Molecular dynamics simulation of the antimicrobial salivary peptide histatin-5 in water and in trifluoroethanol: a microscopic description of the water destructuring effect.	Trifluoroethanol	95-111	histatin 3	Homo sapiens	68-78	
11454169-1	2001	The results of 520 ps molecular dynamics simulation of histatin-5, a small peptide present in human saliva and possessing antimicrobial activity, dissolved in water and in 2,2,2-trifluoroethanol, are reported.	Trifluoroethanol	172-194	histatin 3	Homo sapiens	55-65	
10423240-5	1999	Two-dimensional proton NMR spectroscopy of histatin-5 in a trifluoroethanol/water mixture (a membrane mimetic environment) has been performed and the results analyzed by means of distance geometry and restrained molecular dynamics simulations.	Trifluoroethanol	59-75	histatin 3	Homo sapiens	43-53	
10423240-7	1999	Comparison of the chemical shifts of the individual amino acids in histatin-5 with those recently reported in other solvents indicates that trifluoroethanol/water has a structuring capability somewhere between water and dimethyl sulfoxide.	Trifluoroethanol	140-156	histatin 3	Homo sapiens	67-77