PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28490136-0	2017	Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction.	Catechin	72-80	beta-lactoglobulin	Bos taurus	85-103	
28490136-1	2017	Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow"s milk.	Catechin	16-24	beta-lactoglobulin	Bos taurus	122-140	
32194324-0	2020	Molecular interaction of tea catechin with bovine beta-lactoglobulin: A spectroscopic and in silico studies.	Catechin	29-37	beta-lactoglobulin	Bos taurus	50-68	
32194324-2	2020	Here, we elucidated binding mechanism between frequently consumed polyphenol "tea catechin" and milk protein bovine beta-lactoglobulin (beta-Lg).	Catechin	82-90	beta-lactoglobulin	Bos taurus	116-134	
32194324-2	2020	Here, we elucidated binding mechanism between frequently consumed polyphenol "tea catechin" and milk protein bovine beta-lactoglobulin (beta-Lg).	Catechin	82-90	beta-lactoglobulin	Bos taurus	136-143	
32194324-3	2020	We investigated the conformational changes of beta-Lg due to interaction with catechin using spectroscopic and in silico studies.	Catechin	78-86	beta-lactoglobulin	Bos taurus	46-53	
32194324-4	2020	Fluorescence quenching data (Stern-Volmer quenching constant) revealed that beta-Lg interacted with catechin via dynamic quenching.	Catechin	100-108	beta-lactoglobulin	Bos taurus	76-83	
32194324-5	2020	Thermodynamic data revealed that the interaction between beta-Lg and catechin is endothermic and spontaneously interacted mainly through hydrophobic interactions.	Catechin	69-77	beta-lactoglobulin	Bos taurus	57-64	
32194324-6	2020	The UV-Vis absorption and far-UV circular dichroism (CD) spectroscopy exhibited that the tertiary as well as secondary structure of beta-Lg distorted after interaction with catechin.	Catechin	173-181	beta-lactoglobulin	Bos taurus	132-139	
32194324-7	2020	Molecular docking and simulation studies also confirm that catechin binds at the central cavity of beta-Lg with high affinity (~105 M-1) and hydrophobic interactions play significant role in the formation of a stable beta-Lg-catechin complex.	Catechin	59-67	beta-lactoglobulin	Bos taurus	99-106	
32194324-7	2020	Molecular docking and simulation studies also confirm that catechin binds at the central cavity of beta-Lg with high affinity (~105 M-1) and hydrophobic interactions play significant role in the formation of a stable beta-Lg-catechin complex.	Catechin	59-67	beta-lactoglobulin	Bos taurus	217-224	
32194324-7	2020	Molecular docking and simulation studies also confirm that catechin binds at the central cavity of beta-Lg with high affinity (~105 M-1) and hydrophobic interactions play significant role in the formation of a stable beta-Lg-catechin complex.	Catechin	225-233	beta-lactoglobulin	Bos taurus	99-106	
32194324-7	2020	Molecular docking and simulation studies also confirm that catechin binds at the central cavity of beta-Lg with high affinity (~105 M-1) and hydrophobic interactions play significant role in the formation of a stable beta-Lg-catechin complex.	Catechin	225-233	beta-lactoglobulin	Bos taurus	217-224