Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-152 |
Sentence |
denotes |
NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside. |
T1 |
0-152 |
Sentence |
denotes |
NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside. |
T1 |
0-152 |
Sentence |
denotes |
NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside. |
TextSentencer_T2 |
153-268 |
Sentence |
denotes |
The specific interaction of hevein with GlcNAc-containing oligosaccharides has been analyzed by1H-NMR spectroscopy. |
T2 |
153-268 |
Sentence |
denotes |
The specific interaction of hevein with GlcNAc-containing oligosaccharides has been analyzed by1H-NMR spectroscopy. |
T2 |
153-268 |
Sentence |
denotes |
The specific interaction of hevein with GlcNAc-containing oligosaccharides has been analyzed by1H-NMR spectroscopy. |
TextSentencer_T3 |
269-398 |
Sentence |
denotes |
The association constants for the binding of hevein to a variety of ligands have been estimated from1H-NMR titration experiments. |
T3 |
269-398 |
Sentence |
denotes |
The association constants for the binding of hevein to a variety of ligands have been estimated from1H-NMR titration experiments. |
T3 |
269-398 |
Sentence |
denotes |
The association constants for the binding of hevein to a variety of ligands have been estimated from1H-NMR titration experiments. |
TextSentencer_T4 |
399-617 |
Sentence |
denotes |
The association constants increase in the order GlcNAc-alpha(1-->6)-Man < GlcNAc < benzyl-beta-GlcNAc < p-nitrophenyl-beta-GlcNAc < chitobiose < p-nitrophenyl-beta-chitobioside < methyl-beta-chitobioside < chitotriose. |
T4 |
399-617 |
Sentence |
denotes |
The association constants increase in the order GlcNAc-alpha(1-->6)-Man < GlcNAc < benzyl-beta-GlcNAc < p-nitrophenyl-beta-GlcNAc < chitobiose < p-nitrophenyl-beta-chitobioside < methyl-beta-chitobioside < chitotriose. |
T4 |
399-617 |
Sentence |
denotes |
The association constants increase in the order GlcNAc-alpha(1-->6)-Man < GlcNAc < benzyl-beta-GlcNAc < p-nitrophenyl-beta-GlcNAc < chitobiose < p-nitrophenyl-beta-chitobioside < methyl-beta-chitobioside < chitotriose. |
TextSentencer_T5 |
618-718 |
Sentence |
denotes |
Entropy and enthalpy of binding for different complexes have been obtained from van't Hoff analysis. |
T5 |
618-718 |
Sentence |
denotes |
Entropy and enthalpy of binding for different complexes have been obtained from van't Hoff analysis. |
T5 |
618-718 |
Sentence |
denotes |
Entropy and enthalpy of binding for different complexes have been obtained from van't Hoff analysis. |
TextSentencer_T6 |
719-845 |
Sentence |
denotes |
The driving force for the binding process is provided by a negative DeltaH0which is partially compensated by negative DeltaS0. |
T6 |
719-845 |
Sentence |
denotes |
The driving force for the binding process is provided by a negative DeltaH0which is partially compensated by negative DeltaS0. |
T6 |
719-845 |
Sentence |
denotes |
The driving force for the binding process is provided by a negative DeltaH0which is partially compensated by negative DeltaS0. |
TextSentencer_T7 |
846-974 |
Sentence |
denotes |
These negative signs indicate that hydrogen bonding and van der Waals forces are the major interactions stabilizing the complex. |
T7 |
846-974 |
Sentence |
denotes |
These negative signs indicate that hydrogen bonding and van der Waals forces are the major interactions stabilizing the complex. |
T7 |
846-974 |
Sentence |
denotes |
These negative signs indicate that hydrogen bonding and van der Waals forces are the major interactions stabilizing the complex. |
TextSentencer_T8 |
975-1118 |
Sentence |
denotes |
NOESY NMR experiments in water solution provided 475 accurate protein proton-proton distance constraints after employing the MARDIGRAS program. |
T8 |
975-1118 |
Sentence |
denotes |
NOESY NMR experiments in water solution provided 475 accurate protein proton-proton distance constraints after employing the MARDIGRAS program. |
T8 |
975-1118 |
Sentence |
denotes |
NOESY NMR experiments in water solution provided 475 accurate protein proton-proton distance constraints after employing the MARDIGRAS program. |
TextSentencer_T9 |
1119-1187 |
Sentence |
denotes |
In addition, 15 unambiguous protein/carbohydrate NOEs were detected. |
T9 |
1119-1187 |
Sentence |
denotes |
In addition, 15 unambiguous protein/carbohydrate NOEs were detected. |
T9 |
1119-1187 |
Sentence |
denotes |
In addition, 15 unambiguous protein/carbohydrate NOEs were detected. |
TextSentencer_T10 |
1188-1396 |
Sentence |
denotes |
All the experimental constraints were used in a refinement protocol including restrained molecular dynamics in order to determine the highly refined solution conformation of this protein-carbohydrate complex. |
T10 |
1188-1396 |
Sentence |
denotes |
All the experimental constraints were used in a refinement protocol including restrained molecular dynamics in order to determine the highly refined solution conformation of this protein-carbohydrate complex. |
T10 |
1188-1396 |
Sentence |
denotes |
All the experimental constraints were used in a refinement protocol including restrained molecular dynamics in order to determine the highly refined solution conformation of this protein-carbohydrate complex. |
TextSentencer_T11 |
1397-1578 |
Sentence |
denotes |
With regard to the NMR structure of the free protein, no important changes in the protein nOe's were observed, indicating that carbohydrate-induced conformational changes are small. |
T11 |
1397-1578 |
Sentence |
denotes |
With regard to the NMR structure of the free protein, no important changes in the protein nOe's were observed, indicating that carbohydrate-induced conformational changes are small. |
T11 |
1397-1578 |
Sentence |
denotes |
With regard to the NMR structure of the free protein, no important changes in the protein nOe's were observed, indicating that carbohydrate-induced conformational changes are small. |
TextSentencer_T12 |
1579-1687 |
Sentence |
denotes |
The average backbone rmsd of the 20 refined structures was 0.055 nm, while the heavy atom rmsd was 0.116 nm. |
T12 |
1579-1687 |
Sentence |
denotes |
The average backbone rmsd of the 20 refined structures was 0.055 nm, while the heavy atom rmsd was 0.116 nm. |
T12 |
1579-1687 |
Sentence |
denotes |
The average backbone rmsd of the 20 refined structures was 0.055 nm, while the heavy atom rmsd was 0.116 nm. |
TextSentencer_T13 |
1688-1790 |
Sentence |
denotes |
It can be deduced that both hydrogen bonds and van der Waals contacts confer stability to the complex. |
T13 |
1688-1790 |
Sentence |
denotes |
It can be deduced that both hydrogen bonds and van der Waals contacts confer stability to the complex. |
T13 |
1688-1790 |
Sentence |
denotes |
It can be deduced that both hydrogen bonds and van der Waals contacts confer stability to the complex. |
TextSentencer_T14 |
1791-1972 |
Sentence |
denotes |
A comparison of the three-dimensional structure of hevein in solution to those reported for wheat germ agglutinin (WGA) and hevein itself in the solid state has also been performed. |
T14 |
1791-1972 |
Sentence |
denotes |
A comparison of the three-dimensional structure of hevein in solution to those reported for wheat germ agglutinin (WGA) and hevein itself in the solid state has also been performed. |
T14 |
1791-1972 |
Sentence |
denotes |
A comparison of the three-dimensional structure of hevein in solution to those reported for wheat germ agglutinin (WGA) and hevein itself in the solid state has also been performed. |
TextSentencer_T15 |
1973-2097 |
Sentence |
denotes |
The polypeptide conformation has also been compared to the NMR-derived structure of a smaller antifungical peptide, Ac-AMP2. |
T15 |
1973-2097 |
Sentence |
denotes |
The polypeptide conformation has also been compared to the NMR-derived structure of a smaller antifungical peptide, Ac-AMP2. |
T15 |
1973-2097 |
Sentence |
denotes |
The polypeptide conformation has also been compared to the NMR-derived structure of a smaller antifungical peptide, Ac-AMP2. |