| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-109 |
Sentence |
denotes |
Glycosaminoglycan conformation: do aqueous molecular dynamics simulations agree with x-ray fiber diffraction? |
| T1 |
0-109 |
Sentence |
denotes |
Glycosaminoglycan conformation: do aqueous molecular dynamics simulations agree with x-ray fiber diffraction? |
| T1 |
0-109 |
Sentence |
denotes |
Glycosaminoglycan conformation: do aqueous molecular dynamics simulations agree with x-ray fiber diffraction? |
| TextSentencer_T2 |
110-274 |
Sentence |
denotes |
Glycosaminoglycan-protein interactions are biologically important and require an appreciation of glycan molecular shape in solution, which is presently unavailable. |
| T2 |
110-274 |
Sentence |
denotes |
Glycosaminoglycan-protein interactions are biologically important and require an appreciation of glycan molecular shape in solution, which is presently unavailable. |
| T2 |
110-274 |
Sentence |
denotes |
Glycosaminoglycan-protein interactions are biologically important and require an appreciation of glycan molecular shape in solution, which is presently unavailable. |
| TextSentencer_T3 |
275-432 |
Sentence |
denotes |
In previous studies we found strong similarity between aqueous molecular dynamics (MD) simulations and published x-ray diffraction refinements of hyaluronan. |
| T3 |
275-432 |
Sentence |
denotes |
In previous studies we found strong similarity between aqueous molecular dynamics (MD) simulations and published x-ray diffraction refinements of hyaluronan. |
| T3 |
275-432 |
Sentence |
denotes |
In previous studies we found strong similarity between aqueous molecular dynamics (MD) simulations and published x-ray diffraction refinements of hyaluronan. |
| TextSentencer_T4 |
433-631 |
Sentence |
denotes |
We have applied a similar approach here to chondroitin and dermatan, attempting to clarify some of the issues raised by the x-ray diffraction literature relating to chondroitin and dermatan sulfate. |
| T4 |
433-631 |
Sentence |
denotes |
We have applied a similar approach here to chondroitin and dermatan, attempting to clarify some of the issues raised by the x-ray diffraction literature relating to chondroitin and dermatan sulfate. |
| T4 |
433-631 |
Sentence |
denotes |
We have applied a similar approach here to chondroitin and dermatan, attempting to clarify some of the issues raised by the x-ray diffraction literature relating to chondroitin and dermatan sulfate. |
| TextSentencer_T5 |
632-777 |
Sentence |
denotes |
We predict that chondroitin has the same beta(1-->4) linkage conformation as hyaluronan, and that their average beta(1-->3) conformations differ. |
| T5 |
632-777 |
Sentence |
denotes |
We predict that chondroitin has the same beta(1-->4) linkage conformation as hyaluronan, and that their average beta(1-->3) conformations differ. |
| T5 |
632-777 |
Sentence |
denotes |
We predict that chondroitin has the same beta(1-->4) linkage conformation as hyaluronan, and that their average beta(1-->3) conformations differ. |
| TextSentencer_T6 |
778-1016 |
Sentence |
denotes |
This is explained by changes in hydrogen-bonding across this linkage, resulting from its axial hydroxyl, causing a different sampling of left-handed helices in chondroitin (2.5- to 3.5-fold) as compared with hyaluronan (3.0- to 4.0-fold). |
| T6 |
778-1016 |
Sentence |
denotes |
This is explained by changes in hydrogen-bonding across this linkage, resulting from its axial hydroxyl, causing a different sampling of left-handed helices in chondroitin (2.5- to 3.5-fold) as compared with hyaluronan (3.0- to 4.0-fold). |
| T6 |
778-1016 |
Sentence |
denotes |
This is explained by changes in hydrogen-bonding across this linkage, resulting from its axial hydroxyl, causing a different sampling of left-handed helices in chondroitin (2.5- to 3.5-fold) as compared with hyaluronan (3.0- to 4.0-fold). |
| TextSentencer_T7 |
1017-1124 |
Sentence |
denotes |
Few right-handed helices, which lack intramolecular hydrogen-bonds, were sampled during our MD simulations. |
| T7 |
1017-1124 |
Sentence |
denotes |
Few right-handed helices, which lack intramolecular hydrogen-bonds, were sampled during our MD simulations. |
| T7 |
1017-1124 |
Sentence |
denotes |
Few right-handed helices, which lack intramolecular hydrogen-bonds, were sampled during our MD simulations. |
| TextSentencer_T8 |
1125-1342 |
Sentence |
denotes |
Thus, we propose that the 8-fold helix observed in chondroitin-6-sulfate, represented in the literature as an 8(3) helix (right-handed), though it has never been refined, is more likely to be 8(5) (left-handed) helix. |
| T8 |
1125-1342 |
Sentence |
denotes |
Thus, we propose that the 8-fold helix observed in chondroitin-6-sulfate, represented in the literature as an 8(3) helix (right-handed), though it has never been refined, is more likely to be 8(5) (left-handed) helix. |
| T8 |
1125-1342 |
Sentence |
denotes |
Thus, we propose that the 8-fold helix observed in chondroitin-6-sulfate, represented in the literature as an 8(3) helix (right-handed), though it has never been refined, is more likely to be 8(5) (left-handed) helix. |
| TextSentencer_T9 |
1343-1518 |
Sentence |
denotes |
Molecular dynamics simulations implied that (4)C(1) and (2)S(O), but not (1)C(4), forms of iduronate could be used in refinements of dermatan x-ray fiber diffraction patterns. |
| T9 |
1343-1518 |
Sentence |
denotes |
Molecular dynamics simulations implied that (4)C(1) and (2)S(O), but not (1)C(4), forms of iduronate could be used in refinements of dermatan x-ray fiber diffraction patterns. |
| T9 |
1343-1518 |
Sentence |
denotes |
Molecular dynamics simulations implied that (4)C(1) and (2)S(O), but not (1)C(4), forms of iduronate could be used in refinements of dermatan x-ray fiber diffraction patterns. |
| TextSentencer_T10 |
1519-1676 |
Sentence |
denotes |
Current models of 8-fold dermatan sulfate chains containing (4)C(1) iduronate refine to right-handed helices, which possess no intramolecular hydrogen-bonds. |
| T10 |
1519-1676 |
Sentence |
denotes |
Current models of 8-fold dermatan sulfate chains containing (4)C(1) iduronate refine to right-handed helices, which possess no intramolecular hydrogen-bonds. |
| T10 |
1519-1676 |
Sentence |
denotes |
Current models of 8-fold dermatan sulfate chains containing (4)C(1) iduronate refine to right-handed helices, which possess no intramolecular hydrogen-bonds. |
| TextSentencer_T11 |
1677-1819 |
Sentence |
denotes |
However, MD simulations predict that models containing (2)S(O) iduronate could provide better (8(5) helix) starting structures for refinement. |
| T11 |
1677-1819 |
Sentence |
denotes |
However, MD simulations predict that models containing (2)S(O) iduronate could provide better (8(5) helix) starting structures for refinement. |
| T11 |
1677-1819 |
Sentence |
denotes |
However, MD simulations predict that models containing (2)S(O) iduronate could provide better (8(5) helix) starting structures for refinement. |
| TextSentencer_T12 |
1820-1896 |
Sentence |
denotes |
Thus, the 8-fold dermatan sulfate refinement (8(3) helix) could be in error. |
| T12 |
1820-1896 |
Sentence |
denotes |
Thus, the 8-fold dermatan sulfate refinement (8(3) helix) could be in error. |
| T12 |
1820-1896 |
Sentence |
denotes |
Thus, the 8-fold dermatan sulfate refinement (8(3) helix) could be in error. |