PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 293712-1 1979 In unfolded RNase A there is an interconversion between slow-folding and fast-folding forms (U(S) right harpoon over left harpoon U(F)) that is known to show properties characteristic of proline isomerization in model peptides. isoleucyl-prolyl-proline 187-194 ribonuclease A family member 1, pancreatic Homo sapiens 12-19 293712-3 1979 The U(S) right harpoon over left harpoon U(F) reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.The tyrosine-detected folding kinetics at low temperatures have been compared to those of proline isomerization in unfolded RNase A. isoleucyl-prolyl-proline 123-130 ribonuclease A family member 1, pancreatic Homo sapiens 67-74 293712-3 1979 The U(S) right harpoon over left harpoon U(F) reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.The tyrosine-detected folding kinetics at low temperatures have been compared to those of proline isomerization in unfolded RNase A. isoleucyl-prolyl-proline 123-130 ribonuclease A family member 1, pancreatic Homo sapiens 373-380 293712-3 1979 The U(S) right harpoon over left harpoon U(F) reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.The tyrosine-detected folding kinetics at low temperatures have been compared to those of proline isomerization in unfolded RNase A. isoleucyl-prolyl-proline 212-219 ribonuclease A family member 1, pancreatic Homo sapiens 67-74 293712-3 1979 The U(S) right harpoon over left harpoon U(F) reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.The tyrosine-detected folding kinetics at low temperatures have been compared to those of proline isomerization in unfolded RNase A. isoleucyl-prolyl-proline 212-219 ribonuclease A family member 1, pancreatic Homo sapiens 373-380 293712-3 1979 The U(S) right harpoon over left harpoon U(F) reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.The tyrosine-detected folding kinetics at low temperatures have been compared to those of proline isomerization in unfolded RNase A. isoleucyl-prolyl-proline 212-219 ribonuclease A family member 1, pancreatic Homo sapiens 67-74 293712-3 1979 The U(S) right harpoon over left harpoon U(F) reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.The tyrosine-detected folding kinetics at low temperatures have been compared to those of proline isomerization in unfolded RNase A. isoleucyl-prolyl-proline 212-219 ribonuclease A family member 1, pancreatic Homo sapiens 373-380