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PubMed:8407905 JSONTXT 21 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-122 Sentence denotes Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase.
T1 0-122 Sentence denotes Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase.
T2 123-323 Sentence denotes The irreversible thermal denaturation of the F1 portion of the chloroplast ATP synthase (CF1) was examined by differential scanning calorimetry, ATPase activity loss, and release of bound nucleotides.
T2 123-323 Sentence denotes The irreversible thermal denaturation of the F1 portion of the chloroplast ATP synthase (CF1) was examined by differential scanning calorimetry, ATPase activity loss, and release of bound nucleotides.
T3 324-447 Sentence denotes In nearly all cases, the loss of ATPase activity closely paralleled the temperature dependence of the excess heat capacity.
T3 324-447 Sentence denotes In nearly all cases, the loss of ATPase activity closely paralleled the temperature dependence of the excess heat capacity.
T4 448-573 Sentence denotes Although the irreversible nature of the denaturation precluded thermodynamic interpretation, a kinetic analysis was feasible.
T4 448-573 Sentence denotes Although the irreversible nature of the denaturation precluded thermodynamic interpretation, a kinetic analysis was feasible.
T5 574-649 Sentence denotes A two-state kinetic model was found to fit the calorimetric data very well.
T5 574-649 Sentence denotes A two-state kinetic model was found to fit the calorimetric data very well.
T6 650-896 Sentence denotes The activation energies of thermal denaturation calculated from calorimetric data were very close to those determined from Arrhenius plots of the apparent first-order rate constants of loss of ATPase activity versus reciprocal of the temperature.
T6 650-896 Sentence denotes The activation energies of thermal denaturation calculated from calorimetric data were very close to those determined from Arrhenius plots of the apparent first-order rate constants of loss of ATPase activity versus reciprocal of the temperature.
T7 897-1012 Sentence denotes The nucleotide binding site occupancy profoundly influenced the temperature at which thermal denaturation occurred.
T7 897-1012 Sentence denotes The nucleotide binding site occupancy profoundly influenced the temperature at which thermal denaturation occurred.
T8 1013-1282 Sentence denotes In particular, the temperature at which the maximum in excess heat capacity occurs (Tm) was increased about 8 degrees C by occupancy of tight, noncatalytic ATP binding sites and by an additional 3-4 degrees C by the presence of nucleotides in the medium during heating.
T8 1013-1282 Sentence denotes In particular, the temperature at which the maximum in excess heat capacity occurs (Tm) was increased about 8 degrees C by occupancy of tight, noncatalytic ATP binding sites and by an additional 3-4 degrees C by the presence of nucleotides in the medium during heating.
T9 1283-1436 Sentence denotes The thermal denaturation of CF1, an enzyme composed of nine polypeptide chains, is highly cooperative in that it obeys the simple two-step kinetic model.
T9 1283-1436 Sentence denotes The thermal denaturation of CF1, an enzyme composed of nine polypeptide chains, is highly cooperative in that it obeys the simple two-step kinetic model.
T10 1437-1627 Sentence denotes Since the removal of the epsilon and delta subunits has little effect on thermal denaturation, the major forces that stabilize CF1 must, thus, be between the alpha, beta, and gamma subunits.
T10 1437-1627 Sentence denotes Since the removal of the epsilon and delta subunits has little effect on thermal denaturation, the major forces that stabilize CF1 must, thus, be between the alpha, beta, and gamma subunits.