PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8181470-5	1994	The relative ability to form an alpha helix, assessed by trifluoroethanol/H2O titration, was found to be Elcatonin > sCT > pCT > eCT > hCT.	Trifluoroethanol	57-73	secretin	Homo sapiens	120-123	
8181470-6	1994	In Elcatonin, sCT, pCT and eCT the four alpha-helical turns were promoted almost completely in a single step, between 0 and 35% trifluoroethanol, unlike hCT where helical structure formation has been reported to involve two steps over the whole trifluoroethanol/H2O range [Arvinte, T. & Drake, A. F. (1993) J. Biol.	Trifluoroethanol	128-144	secretin	Homo sapiens	14-17	
8181470-6	1994	In Elcatonin, sCT, pCT and eCT the four alpha-helical turns were promoted almost completely in a single step, between 0 and 35% trifluoroethanol, unlike hCT where helical structure formation has been reported to involve two steps over the whole trifluoroethanol/H2O range [Arvinte, T. & Drake, A. F. (1993) J. Biol.	Trifluoroethanol	245-261	secretin	Homo sapiens	14-17	
2883029-2	1987	The solution conformation of the 27 residue polypeptide hormone secretin has been investigated by 1H-NMR spectroscopy under conditions where it adopts a fully ordered structure as judged by circular dichroism spectroscopy, namely in an aqueous solution of 40% (v/v) trifluoroethanol.	Trifluoroethanol	266-282	secretin	Homo sapiens	64-72	
8454613-6	1993	In 2,2,2-trifluoroethanol (TFE)/water mixtures the alpha-helix formation for both hCT and sCT is a two-step process.	Trifluoroethanol	3-25	secretin	Homo sapiens	90-93	
8454613-6	1993	In 2,2,2-trifluoroethanol (TFE)/water mixtures the alpha-helix formation for both hCT and sCT is a two-step process.	Trifluoroethanol	27-30	secretin	Homo sapiens	90-93	
8454613-7	1993	The first alpha-helix formation step occurs at lower TFE concentrations (less than 11 mol% TFE for hCT and 6 mol% TFE for sCT).	Trifluoroethanol	53-56	secretin	Homo sapiens	122-125