PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
188485-4	1976	In the complexes formed by the association of apoC-III with single-bilayer vesicles, the alpha-helical content of the peptide backbone and the apolarity of the environment around the tryptophan residues are greater than that observed in the complexes formed with the multibilayer vesicles.	Tryptophan	183-193	apolipoprotein C3	Homo sapiens	46-54	
27529357-0	2016	Apolipoprotein C-III Nanodiscs Studied by Site-Specific Tryptophan Fluorescence.	Tryptophan	56-66	apolipoprotein C3	Homo sapiens	0-20	
27529357-8	2016	On the basis of Trp spectral comparisons of ApoC-III in micellar and vesicle environments, ApoC-III binding within nanodiscs more closely resembles a bilayer-bound state.	Tryptophan	16-19	apolipoprotein C3	Homo sapiens	91-99	
26301570-0	2015	Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III.	Tryptophan	0-10	apolipoprotein C3	Homo sapiens	71-91	
26301570-10	2015	Based on Trp spectral differences between ApoCIII binding to phospholipid vesicles and sodium dodecyl sulfate micelles, we suggest that ApoCIII adopts an alternate helical conformation on the bilayer which could have functional implications.	Tryptophan	9-12	apolipoprotein C3	Homo sapiens	136-143