PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29272129-3	2018	The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively.	Glutamic Acid	83-92	lactalbumin alpha	Homo sapiens	152-169	
29272129-3	2018	The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively.	Glutamic Acid	83-92	lactalbumin alpha	Homo sapiens	171-179	
29272129-3	2018	The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively.	Glutamic Acid	94-97	lactalbumin alpha	Homo sapiens	152-169	
29272129-3	2018	The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively.	Glutamic Acid	94-97	lactalbumin alpha	Homo sapiens	171-179	
29272129-10	2018	However, urea subverts the Glu-induced intermediate formed by alpha-LA, whereas it only slightly destabilizes in the case of RNase A which has a positive surface charge and could possess charge-charge interactions with Glu.	Glutamic Acid	27-30	lactalbumin alpha	Homo sapiens	62-70	
29272129-14	2018	The extent of stability exerted by Glu is higher for RNase A at higher temperature, whereas it provides more stability for alpha-LA at lower temperature.	Glutamic Acid	35-38	lactalbumin alpha	Homo sapiens	123-131