> top > docs > PubMed:7251592 > annotations

PubMed:7251592 JSONTXT

Annnotations TAB JSON ListView MergeView

sentences

Id Subject Object Predicate Lexical cue
T1 0-41 Sentence denotes The stabilization of proteins by sucrose.
T2 42-151 Sentence denotes The interactions between proteins and solvent components have been investigated for the sucrose/water system.
T3 152-328 Sentence denotes Thermodynamic and kinetic measurements of the thermal unfolding of alpha-chymotrypsin, chymotrypsinogen, and ribonuclease were performed as a function of sucrose concentration.
T4 329-496 Sentence denotes The alteration in protein-solvent interactions in the presence of sucrose was also studied by density measurements and analyzed by multicomponent thermodynamic theory.
T5 497-662 Sentence denotes Sucrose does not induce a conformational change in three proteins studied, although it does induce a small change in the circular dichroism spectrum of ribonuclease.
T6 663-856 Sentence denotes The enthalpy of thermal unfolding shows little dependence on the concentration of sucrose, while the apparent activation energy of the unfolding process is increased by the addition of sucrose.
T7 857-1027 Sentence denotes The results from the protein-solvent interaction study indicate that sucrose is preferentially excluded from the protein domain, increasing the free energy of the system.
T8 1028-1195 Sentence denotes Thermodynamically this leads to protein stabilization since the unfolded state of the protein becomes thermodynamically even less favorable in the presence of sucrose.
T9 1196-1447 Sentence denotes The exclusion of sucrose from the protein domain seems to be related to the higher cohesive force of the sucrose water solvent system since all the experimental observations can be correlated with the effect of sucrose on the surface tension of water.
T1 0-41 Sentence denotes The stabilization of proteins by sucrose.
T2 42-151 Sentence denotes The interactions between proteins and solvent components have been investigated for the sucrose/water system.
T3 152-328 Sentence denotes Thermodynamic and kinetic measurements of the thermal unfolding of alpha-chymotrypsin, chymotrypsinogen, and ribonuclease were performed as a function of sucrose concentration.
T4 329-496 Sentence denotes The alteration in protein-solvent interactions in the presence of sucrose was also studied by density measurements and analyzed by multicomponent thermodynamic theory.
T5 497-662 Sentence denotes Sucrose does not induce a conformational change in three proteins studied, although it does induce a small change in the circular dichroism spectrum of ribonuclease.
T6 663-856 Sentence denotes The enthalpy of thermal unfolding shows little dependence on the concentration of sucrose, while the apparent activation energy of the unfolding process is increased by the addition of sucrose.
T7 857-1027 Sentence denotes The results from the protein-solvent interaction study indicate that sucrose is preferentially excluded from the protein domain, increasing the free energy of the system.
T8 1028-1195 Sentence denotes Thermodynamically this leads to protein stabilization since the unfolded state of the protein becomes thermodynamically even less favorable in the presence of sucrose.
T9 1196-1447 Sentence denotes The exclusion of sucrose from the protein domain seems to be related to the higher cohesive force of the sucrose water solvent system since all the experimental observations can be correlated with the effect of sucrose on the surface tension of water.