PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25974045-3	2015	Thermal transitions of alpha-lactalbumin and beta-lactoglobulin components of BWP included water-content-dependent endothermic but reversible dehydration and denaturation, and exothermic and irreversible aggregation.	Water	91-96	lactalbumin alpha	Bos taurus	23-40	
32036330-0	2020	Camel alpha-lactalbumin at the oil-water interface: Effect of protein concentration and pH change on surface characteristics and emulsifying properties.	Water	35-40	lactalbumin alpha	Bos taurus	6-23	
27137845-0	2016	Dynamics of Hydration Water around Native and Misfolded alpha-Lactalbumin.	Water	22-27	lactalbumin alpha	Bos taurus	56-73	
27137845-2	2016	We investigate water dynamics around bovine alpha-lactalbumin by combining molecular dynamics simulations with polarization-resolved femtosecond infrared (fs-IR) spectroscopy.	Water	15-20	lactalbumin alpha	Bos taurus	44-61	
17676769-1	2007	Prolonged heating of holo bovine alpha-lactalbumin (BLA) at 80 degrees C in pH 7 phosphate buffer in the absence of a thiol initiator improves the surface activity of the protein at the air:water interface, as determined by surface tension measurements.	Water	190-195	lactalbumin alpha	Bos taurus	33-50	
12139936-1	2002	The interaction of bovine alpha-lactalbumin (BLA) with negatively charged phospholipid bilayers was studied by NMR monitored 1H exchange to characterize the conformational transition that enables a water-soluble protein to associate with and partially insert into a membrane.	Water	198-203	lactalbumin alpha	Bos taurus	26-43