PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12876309-2	2003	Therefore, the BLG fatty-acid equilibrium has been tackled by exploiting the competition between fatty acids and ANS, a widely used fluorescent hydrophobic probe, whose binding sites on the protein have been characterized recently.	1-anilino-8-naphthalenesulfonate	113-116	beta-lactoglobulin	Bos taurus	15-18	
235319-1	1975	A conformational change at low pH in bovine beta-lactoglobulin A has been studied by intrinsic fluorescence and fluorescence of the bound dye 8-anilinonaphthalene-1-sulphonate.	1-anilino-8-naphthalenesulfonate	142-175	beta-lactoglobulin	Bos taurus	44-62	
22927212-3	2013	Here, we used a method we named CS-PCA, a principal component analysis (PCA) of chemical shift (CS) data, to analyze the interaction between bovine beta-lactoglobulin (betaLG) and 1-anilinonaphthalene-8-sulfonate (ANS), which is a multiple-ligand-binding system.	1-anilino-8-naphthalenesulfonate	214-217	beta-lactoglobulin	Bos taurus	148-166	
18590743-2	2008	We used noncovalent labeling with thioflavin T and 1-anilino-8-naphthalenesulfonate to follow the conformational changes occurring in beta-lactoglobulin during aggregation using time resolved luminescence.	1-anilino-8-naphthalenesulfonate	51-83	beta-lactoglobulin	Bos taurus	134-152	
18590743-3	2008	1-Anilino-8-naphthalenesulfonate monitored the involvement of the hydrophobic core/calyx of beta-lactoglobulin in the aggregation process.	1-anilino-8-naphthalenesulfonate	0-32	beta-lactoglobulin	Bos taurus	92-110	
20875748-4	2011	In this article, interactions between lysine modified bovine beta-lactoglobulin (beta-lg) and a hydrophobic fluorescence probe, 1-anilinonapthalene-8-sulfonate (ANS), have been studied with the help of fluorescence resonance energy transfer (FRET) process.	1-anilino-8-naphthalenesulfonate	161-164	beta-lactoglobulin	Bos taurus	61-79	
20875748-4	2011	In this article, interactions between lysine modified bovine beta-lactoglobulin (beta-lg) and a hydrophobic fluorescence probe, 1-anilinonapthalene-8-sulfonate (ANS), have been studied with the help of fluorescence resonance energy transfer (FRET) process.	1-anilino-8-naphthalenesulfonate	161-164	beta-lactoglobulin	Bos taurus	81-88	
20875748-9	2011	Furthermore, time resolved studies showed that in the derivatives, hydrophobic cavities of beta-lg were collapsed so that ANS failed to recognize the deep interior pockets leading to the loss of longer lifetime component.	1-anilino-8-naphthalenesulfonate	122-125	beta-lactoglobulin	Bos taurus	91-98	
12876309-3	2003	Two lifetime decays of the ANS-BLG complex have been found; the longer one has been attributed to the internal binding site and the shorter one to the external site.	1-anilino-8-naphthalenesulfonate	27-30	beta-lactoglobulin	Bos taurus	31-34	
12876309-6	2003	An estimate of the acid-binding affinities for BLG has been obtained by implementing the fitting of the bound ANS intensities with a competitive binding model.	1-anilino-8-naphthalenesulfonate	110-113	beta-lactoglobulin	Bos taurus	47-50	
10390860-5	1999	Although the bulk of the present work is dedicated to the characterization of Cys-acrylamide adducts, the preliminary data on noncovalent complexes between two of those proteins and 8-anilinonaphthalene-1-sulfonic acid (ANS) were easily observed under electrospray conditions, while under MALDI-TOF conditions only the complex with beta-lactoglobulin B was clearly evident.	1-anilino-8-naphthalenesulfonate	182-218	beta-lactoglobulin	Bos taurus	332-350