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sentences

Id Subject Object Predicate Lexical cue
T1 0-118 Sentence denotes The rates of commitment to renaturation of rhodanese and glutamine synthetase in the presence of the groE chaperonins.
T2 119-318 Sentence denotes Current models of chaperonin-assisted folding suggest that proteins undergo multiple rounds of binding and release before they are released in a form that is committed to folding to the native state.
T3 319-506 Sentence denotes Using immunoprecipitation techniques, we have determined the rates at which rhodanese and glutamine synthetase (GS) are released from groEL in a form committed to refold to active enzyme.
T4 507-708 Sentence denotes Rhodanese and glutamine synthetase were chosen as substrates because they exhibit different solution requirements for the chaperonin system and they form stable "folding arrested" complexes with groEL.
T5 709-872 Sentence denotes At various times during the groE-dependent renaturations, groEL was rapidly removed from the renaturation mixture by immunoprecipitation and centrifugation (30 s).
T6 873-982 Sentence denotes The conformers that are committed to the native state remained in the supernatant and were assayed after 1 h.
T7 983-1159 Sentence denotes At 25 degrees C, the rate profiles indicate the release and commitment to folding of GS to its native state occurs far earlier (t1/2 < 1 min) than for rhodanese (t1/2 = 5 min).
T8 1160-1326 Sentence denotes In light of previous results, it appears that GS monomers can attain a groE-independent assembly competent conformation after a brief interaction with the chaperonin.
T9 1327-1470 Sentence denotes In contrast, the renaturation rate for rhodanese with the groE chaperonins mirrored the committed renaturation rates following groEL depletion.
T10 1471-1629 Sentence denotes This suggests that rhodanese must interact with groEL throughout most of its folding reaction before it acquires a folding competent (groE independent) state.
T11 1630-1752 Sentence denotes If current models of chaperonin mechanism are correct, rhodanese undergoes more rebinding and release cycles than does GS.
T12 1753-1987 Sentence denotes Structurally, the degree of cycling and hence the rate of commitment to folding to the active form are probably dictated by the hydrophobic nature, number, and lifetimes of the folding intermediates that interact with the chaperonins.
T1 0-118 Sentence denotes The rates of commitment to renaturation of rhodanese and glutamine synthetase in the presence of the groE chaperonins.
T2 119-318 Sentence denotes Current models of chaperonin-assisted folding suggest that proteins undergo multiple rounds of binding and release before they are released in a form that is committed to folding to the native state.
T3 319-506 Sentence denotes Using immunoprecipitation techniques, we have determined the rates at which rhodanese and glutamine synthetase (GS) are released from groEL in a form committed to refold to active enzyme.
T4 507-708 Sentence denotes Rhodanese and glutamine synthetase were chosen as substrates because they exhibit different solution requirements for the chaperonin system and they form stable "folding arrested" complexes with groEL.
T5 709-872 Sentence denotes At various times during the groE-dependent renaturations, groEL was rapidly removed from the renaturation mixture by immunoprecipitation and centrifugation (30 s).
T6 873-982 Sentence denotes The conformers that are committed to the native state remained in the supernatant and were assayed after 1 h.
T7 983-1159 Sentence denotes At 25 degrees C, the rate profiles indicate the release and commitment to folding of GS to its native state occurs far earlier (t1/2 < 1 min) than for rhodanese (t1/2 = 5 min).
T8 1160-1326 Sentence denotes In light of previous results, it appears that GS monomers can attain a groE-independent assembly competent conformation after a brief interaction with the chaperonin.
T9 1327-1470 Sentence denotes In contrast, the renaturation rate for rhodanese with the groE chaperonins mirrored the committed renaturation rates following groEL depletion.
T10 1471-1629 Sentence denotes This suggests that rhodanese must interact with groEL throughout most of its folding reaction before it acquires a folding competent (groE independent) state.
T11 1630-1752 Sentence denotes If current models of chaperonin mechanism are correct, rhodanese undergoes more rebinding and release cycles than does GS.
T12 1753-1987 Sentence denotes Structurally, the degree of cycling and hence the rate of commitment to folding to the active form are probably dictated by the hydrophobic nature, number, and lifetimes of the folding intermediates that interact with the chaperonins.

AIMed

Id Subject Object Predicate Lexical cue
T1 43-52 protein denotes rhodanese
T2 57-77 protein denotes glutamine synthetase
T3 395-404 protein denotes rhodanese
T4 409-429 protein denotes glutamine synthetase
T5 431-433 protein denotes GS
T6 453-458 protein denotes groEL
T7 507-516 protein denotes Rhodanese
T8 521-541 protein denotes glutamine synthetase
T9 702-707 protein denotes groEL
T10 767-772 protein denotes groEL
T11 1068-1070 protein denotes GS
T12 1134-1143 protein denotes rhodanese
T13 1206-1208 protein denotes GS
T14 1366-1375 protein denotes rhodanese
T15 1454-1459 protein denotes groEL
T16 1490-1499 protein denotes rhodanese
T17 1519-1524 protein denotes groEL
T18 1685-1694 protein denotes rhodanese
T19 1749-1751 protein denotes GS