| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-136 |
Sentence |
denotes |
NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans. |
| TextSentencer_T2 |
137-296 |
Sentence |
denotes |
Complete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. |
| TextSentencer_T3 |
297-602 |
Sentence |
denotes |
These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1-->3) Galpbeta(1-->3)Galpbeta(1-->4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1-->3)Galpbeta(1-->3)Galpbeta(1-->4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1-->3)Galpbeta(1-->3)Galpbeta(1-->4)X ylpbeta)-Gly (2). |
| TextSentencer_T4 |
603-707 |
Sentence |
denotes |
The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. |
| TextSentencer_T5 |
708-929 |
Sentence |
denotes |
Distance geometry/simulated annealing calculations using 2D NOESY derived distance constraints yielded a single family of structures for the tetrasaccharide moiety, with well defined interglycosidic linkage conformations. |
| TextSentencer_T6 |
930-1199 |
Sentence |
denotes |
The straight phi torsion angles of the glycosidic C1'-O1 bonds showed a strict preference for the -sc range whereas the psi torsion angles (O1-Cn) exhibited dependence upon the interglycosidic linkage position (-ac for beta(1-->3) linkage, +ac for beta(1-->4) linkage). |
| TextSentencer_T7 |
1200-1293 |
Sentence |
denotes |
The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. |
| TextSentencer_T8 |
1294-1592 |
Sentence |
denotes |
The presence of strong daN (i, i+1) NOE contacts, and the general absence of dNN (i, i+1) contacts (except for a weak Ser-5/Gly-6 dNN contact) and the dbN (i, i+1) contacts (except for Ser-1/Gly-2) in the ROESY spectrum, suggest that the backbone for 1 is predominantly in an extended conformation. |
| TextSentencer_T9 |
1593-1817 |
Sentence |
denotes |
A comparison of the ROESY data for 1 with those obtained from the unglycosylated hexapeptide (3) of the same sequence suggests that glycosylation has only a marginal influence on the backbone conformation of the hexapeptide. |
| T1 |
0-136 |
Sentence |
denotes |
NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans. |
| T2 |
137-296 |
Sentence |
denotes |
Complete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. |
| T3 |
297-602 |
Sentence |
denotes |
These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1-->3) Galpbeta(1-->3)Galpbeta(1-->4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1-->3)Galpbeta(1-->3)Galpbeta(1-->4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1-->3)Galpbeta(1-->3)Galpbeta(1-->4)X ylpbeta)-Gly (2). |
| T4 |
603-707 |
Sentence |
denotes |
The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. |
| T5 |
708-929 |
Sentence |
denotes |
Distance geometry/simulated annealing calculations using 2D NOESY derived distance constraints yielded a single family of structures for the tetrasaccharide moiety, with well defined interglycosidic linkage conformations. |
| T6 |
930-1199 |
Sentence |
denotes |
The straight phi torsion angles of the glycosidic C1'-O1 bonds showed a strict preference for the -sc range whereas the psi torsion angles (O1-Cn) exhibited dependence upon the interglycosidic linkage position (-ac for beta(1-->3) linkage, +ac for beta(1-->4) linkage). |
| T7 |
1200-1293 |
Sentence |
denotes |
The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. |
| T8 |
1294-1592 |
Sentence |
denotes |
The presence of strong daN (i, i+1) NOE contacts, and the general absence of dNN (i, i+1) contacts (except for a weak Ser-5/Gly-6 dNN contact) and the dbN (i, i+1) contacts (except for Ser-1/Gly-2) in the ROESY spectrum, suggest that the backbone for 1 is predominantly in an extended conformation. |
| T9 |
1593-1817 |
Sentence |
denotes |
A comparison of the ROESY data for 1 with those obtained from the unglycosylated hexapeptide (3) of the same sequence suggests that glycosylation has only a marginal influence on the backbone conformation of the hexapeptide. |
| T1 |
0-136 |
Sentence |
denotes |
NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans. |
| T2 |
137-296 |
Sentence |
denotes |
Complete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. |
| T3 |
297-602 |
Sentence |
denotes |
These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1-->3) Galpbeta(1-->3)Galpbeta(1-->4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1-->3)Galpbeta(1-->3)Galpbeta(1-->4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1-->3)Galpbeta(1-->3)Galpbeta(1-->4)X ylpbeta)-Gly (2). |
| T4 |
603-707 |
Sentence |
denotes |
The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. |
| T5 |
708-929 |
Sentence |
denotes |
Distance geometry/simulated annealing calculations using 2D NOESY derived distance constraints yielded a single family of structures for the tetrasaccharide moiety, with well defined interglycosidic linkage conformations. |
| T6 |
930-1199 |
Sentence |
denotes |
The straight phi torsion angles of the glycosidic C1'-O1 bonds showed a strict preference for the -sc range whereas the psi torsion angles (O1-Cn) exhibited dependence upon the interglycosidic linkage position (-ac for beta(1-->3) linkage, +ac for beta(1-->4) linkage). |
| T7 |
1200-1293 |
Sentence |
denotes |
The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. |
| T8 |
1294-1592 |
Sentence |
denotes |
The presence of strong daN (i, i+1) NOE contacts, and the general absence of dNN (i, i+1) contacts (except for a weak Ser-5/Gly-6 dNN contact) and the dbN (i, i+1) contacts (except for Ser-1/Gly-2) in the ROESY spectrum, suggest that the backbone for 1 is predominantly in an extended conformation. |
| T9 |
1593-1817 |
Sentence |
denotes |
A comparison of the ROESY data for 1 with those obtained from the unglycosylated hexapeptide (3) of the same sequence suggests that glycosylation has only a marginal influence on the backbone conformation of the hexapeptide. |
