PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12533538-2	2003	By lyophilizing RNase A from 40% acetic acid solutions, two dimeric aggregates, the "minor" and "major" dimers (named here N-dimer and C-dimer, respectively), form by 3D domain swapping at a ratio of 1:4.	Acetic Acid	33-44	ribonuclease A family member 1, pancreatic	Homo sapiens	16-23	
10736157-7	2000	Moreover, the HP-RNase dimers were found to be over 4.6 orders of magnitude more stable than the dimers of bovine pancreatic RNase A obtained by lyophilization from acetic acid (K(d) > 73 mM).	Acetic Acid	165-176	ribonuclease A family member 1, pancreatic	Homo sapiens	14-22	
10648807-3	2000	240, 2868-3874) observed that dimeric RNase A prepared by lyophilization from acetic acid could be separated into two forms.	Acetic Acid	78-89	ribonuclease A family member 1, pancreatic	Homo sapiens	38-45	
20085318-0	2010	NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping.	Acetic Acid	66-77	ribonuclease A family member 1, pancreatic	Homo sapiens	30-37	
20085318-3	2010	RNase A oligomerization is induced by 40% acetic acid, which has been assumed to mildly unfold the protein by detaching the terminal segments and consequently facilitating intersubunit swapping, once the acetic acid is removed by lyophilization and the protein is redissolved in a benign buffer.	Acetic Acid	42-53	ribonuclease A family member 1, pancreatic	Homo sapiens	0-7	
20085318-3	2010	RNase A oligomerization is induced by 40% acetic acid, which has been assumed to mildly unfold the protein by detaching the terminal segments and consequently facilitating intersubunit swapping, once the acetic acid is removed by lyophilization and the protein is redissolved in a benign buffer.	Acetic Acid	204-215	ribonuclease A family member 1, pancreatic	Homo sapiens	0-7	
20085318-4	2010	Using UV difference, near UV circular dichroism, folding kinetics, and multidimensional heteronuclear NMR spectroscopy, the conformation of RNase A in 40% acetic acid and in 8 M urea has been characterized.	Acetic Acid	155-166	ribonuclease A family member 1, pancreatic	Homo sapiens	140-147	
20085318-5	2010	These studies demonstrate that RNase A is chiefly unfolded in 40% acetic acid; it partially retains the native helices, whereas the beta-sheet is fully denatured and all X-Pro peptide bonds are predominantly in the trans conformation.	Acetic Acid	66-77	ribonuclease A family member 1, pancreatic	Homo sapiens	31-38