PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10194351-4	1999	The fluorescence emission wavelength maximum (excitation 295 nm) of the tryptophans in apoA-I (W74 and W107) displayed a marked blue shift in both the lipid-free (331 nm) and HDL-bound (329 nm) states, compared to free tryptophan in solution.	Tryptophan	72-82	apolipoprotein AI	Gallus gallus	87-93	
10194351-12	1999	5-DSA was the most effective quencher, suggesting that apoA-I tryptophan residues localize near the surface monolayer, providing a structural rationale for the reversibility of apoA-I-lipoprotein particle interactions.	Tryptophan	62-72	apolipoprotein AI	Gallus gallus	55-61	
10194351-12	1999	5-DSA was the most effective quencher, suggesting that apoA-I tryptophan residues localize near the surface monolayer, providing a structural rationale for the reversibility of apoA-I-lipoprotein particle interactions.	Tryptophan	62-72	apolipoprotein AI	Gallus gallus	177-183	
9349556-3	1997	Both treatments produced several physical and chemical changes in the HDLs, i.e., formation of lipid peroxides, enlargement of HDL diameters, an increased exposure of the tryptophan groups of the apolipoprotein A-I to a more hydrophilic environment, formation of bityrosines, and cross-linking of apolipoprotein A-I.	Tryptophan	171-181	apolipoprotein AI	Gallus gallus	196-214	
10194351-4	1999	The fluorescence emission wavelength maximum (excitation 295 nm) of the tryptophans in apoA-I (W74 and W107) displayed a marked blue shift in both the lipid-free (331 nm) and HDL-bound (329 nm) states, compared to free tryptophan in solution.	Tryptophan	72-83	apolipoprotein AI	Gallus gallus	87-93