PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10651809-8	2000	In studies of apoLp-III-DMPC disc complexes, far-UV CD spectroscopy revealed an increase in alpha-helix content to approximately 85% and a ninefold increase in the GdnHCl-induced denaturation transition midpoint to 3 M. In studies of lipid interaction, apoLp-III was shown to disrupt both negatively charged and zwitterionic phospholipid bilayer vesicles, transforming them into discoidal complexes.	Dimyristoylphosphatidylcholine	24-28	apolipophorin III	Bombyx mori	14-23	
10651809-8	2000	In studies of apoLp-III-DMPC disc complexes, far-UV CD spectroscopy revealed an increase in alpha-helix content to approximately 85% and a ninefold increase in the GdnHCl-induced denaturation transition midpoint to 3 M. In studies of lipid interaction, apoLp-III was shown to disrupt both negatively charged and zwitterionic phospholipid bilayer vesicles, transforming them into discoidal complexes.	Dimyristoylphosphatidylcholine	24-28	apolipophorin III	Bombyx mori	253-262	
10651809-9	2000	Characterization of apoLp-III-DMPC discs, using 5-doxyl or 12-doxyl stearic acid as lipid-based quenching agents, revealed that Trp40 localizes near the phospholipid polar head groups.	Dimyristoylphosphatidylcholine	30-34	apolipophorin III	Bombyx mori	20-29	
10651809-10	2000	KSV values for acrylamide and KI quenching of intrinsic fluorescence of apoLp-III-DMPC discs indicate that Trp40 is embedded in the lipid milieu, with little or no accessibility to the aqueous quenchers.	Dimyristoylphosphatidylcholine	82-86	apolipophorin III	Bombyx mori	72-81	
10651809-3	2000	Near-UV CD spectra obtained in buffer or complexed with dimyristoylglycerophosphocholine (DMPC), provided evidence that apoLp-III alpha-helices reorient upon interaction with lipid, indicative of a protein conformational change.	Dimyristoylphosphatidylcholine	56-88	apolipophorin III	Bombyx mori	120-129	
10651809-3	2000	Near-UV CD spectra obtained in buffer or complexed with dimyristoylglycerophosphocholine (DMPC), provided evidence that apoLp-III alpha-helices reorient upon interaction with lipid, indicative of a protein conformational change.	Dimyristoylphosphatidylcholine	90-94	apolipophorin III	Bombyx mori	120-129