PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
283390-0	1978	Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization.	Proline	102-109	ribonuclease A family member 1, pancreatic	Homo sapiens	63-70	
283390-10	1978	Earlier data, showing that the kinetic properties of the U(1) right arrow over left arrow U(2) reaction in refolding conditions differ from those of proline isomerization, can be explained if there is kinetic coupling between early steps in the folding of U(1) and its conversion to U(2).The existence of two acid-catalyzed reactions that are distinguished by the HClO(4) concentration at which catalysis begins suggests that at least two essential proline residues produce slow-folding species of RNase A by isomerization after unfolding.	Proline	149-156	ribonuclease A family member 1, pancreatic	Homo sapiens	498-505	
283390-10	1978	Earlier data, showing that the kinetic properties of the U(1) right arrow over left arrow U(2) reaction in refolding conditions differ from those of proline isomerization, can be explained if there is kinetic coupling between early steps in the folding of U(1) and its conversion to U(2).The existence of two acid-catalyzed reactions that are distinguished by the HClO(4) concentration at which catalysis begins suggests that at least two essential proline residues produce slow-folding species of RNase A by isomerization after unfolding.	Proline	449-456	ribonuclease A family member 1, pancreatic	Homo sapiens	498-505