PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7729510-1	1995	Horse heart cytochrome c is cleaved by thermolysin in 50% aqueous TFE (v/v) at neutral pH (25 degrees C, 24 h) at the Gly56-Ile57 peptide bond of the 104-residue chain of the protein.	Polytetrafluoroethylene	66-69	cytochrome c, somatic	Equus caballus	12-24	
7729510-3	1995	On the other hand, in buffer only and in the absence of TFE, cytochrome c is digested by thermolysin to numerous small peptides.	Polytetrafluoroethylene	56-59	cytochrome c, somatic	Equus caballus	61-73	
7729510-5	1995	It is proposed that the highly helical secondary structure acquired by cytochrome c when dissolved in aqueous TFE hampers binding and adaptation of the protein substrate at the active site of the protease and that peptide bond fission occurs at flexible chain segments characterized by a low alpha-helix propensity.	Polytetrafluoroethylene	110-113	cytochrome c, somatic	Equus caballus	71-83