PubMed:10362836 JSON TXT

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Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":104,"end":121},"obj":"http://purl.obolibrary.org/obo/MAT_0000301"},{"id":"T2","span":{"begin":264,"end":281},"obj":"http://purl.obolibrary.org/obo/MAT_0000301"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":137,"end":296},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":297,"end":602},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":603,"end":707},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":708,"end":929},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":930,"end":1199},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1200,"end":1293},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1294,"end":1592},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1593,"end":1817},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"T2","span":{"begin":137,"end":296},"obj":"Sentence"},{"id":"T3","span":{"begin":297,"end":602},"obj":"Sentence"},{"id":"T4","span":{"begin":603,"end":707},"obj":"Sentence"},{"id":"T5","span":{"begin":708,"end":929},"obj":"Sentence"},{"id":"T6","span":{"begin":930,"end":1199},"obj":"Sentence"},{"id":"T7","span":{"begin":1200,"end":1293},"obj":"Sentence"},{"id":"T8","span":{"begin":1294,"end":1592},"obj":"Sentence"},{"id":"T9","span":{"begin":1593,"end":1817},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"T2","span":{"begin":137,"end":296},"obj":"Sentence"},{"id":"T3","span":{"begin":297,"end":602},"obj":"Sentence"},{"id":"T4","span":{"begin":603,"end":707},"obj":"Sentence"},{"id":"T5","span":{"begin":708,"end":929},"obj":"Sentence"},{"id":"T6","span":{"begin":930,"end":1199},"obj":"Sentence"},{"id":"T7","span":{"begin":1200,"end":1293},"obj":"Sentence"},{"id":"T8","span":{"begin":1294,"end":1592},"obj":"Sentence"},{"id":"T9","span":{"begin":1593,"end":1817},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

GlycoBiology-cGGDB

{"project":"GlycoBiology-cGGDB","denotations":[{"id":"_T1","span":{"begin":1418,"end":1423},"obj":"http://jcggdb.jp/cggdb/entry.action?jcg_id=JCEG216"},{"id":"_T2","span":{"begin":1485,"end":1490},"obj":"http://jcggdb.jp/cggdb/entry.action?jcg_id=JCEG085"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":1149,"end":1155},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T2","span":{"begin":1178,"end":1184},"obj":"http://www.uniprot.org/uniprot/Q92988"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":1029,"end":1031},"obj":"http://www.uniprot.org/uniprot/Q9JLI6"},{"id":"T2","span":{"begin":1276,"end":1278},"obj":"http://www.uniprot.org/uniprot/Q9JLI6"},{"id":"T3","span":{"begin":1142,"end":1144},"obj":"http://www.uniprot.org/uniprot/Q91V92"},{"id":"T4","span":{"begin":1171,"end":1173},"obj":"http://www.uniprot.org/uniprot/Q91V92"},{"id":"T5","span":{"begin":1290,"end":1292},"obj":"http://www.uniprot.org/uniprot/Q91V92"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":115,"end":121},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T2","span":{"begin":275,"end":281},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T3","span":{"begin":483,"end":487},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T4","span":{"begin":483,"end":487},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T5","span":{"begin":717,"end":725},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1369226"},{"id":"T6","span":{"begin":1149,"end":1153},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T7","span":{"begin":1149,"end":1153},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T8","span":{"begin":1178,"end":1182},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T9","span":{"begin":1178,"end":1182},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":1142,"end":1144},"obj":"http://purl.obolibrary.org/obo/GO_0003987"},{"id":"T2","span":{"begin":1142,"end":1144},"obj":"http://purl.obolibrary.org/obo/GO_0043884"},{"id":"T3","span":{"begin":1171,"end":1173},"obj":"http://purl.obolibrary.org/obo/GO_0003987"},{"id":"T4","span":{"begin":1171,"end":1173},"obj":"http://purl.obolibrary.org/obo/GO_0043884"},{"id":"T5","span":{"begin":1290,"end":1292},"obj":"http://purl.obolibrary.org/obo/GO_0003987"},{"id":"T6","span":{"begin":1290,"end":1292},"obj":"http://purl.obolibrary.org/obo/GO_0043884"},{"id":"T7","span":{"begin":1725,"end":1738},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":353,"end":356},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T2","span":{"begin":418,"end":421},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T3","span":{"begin":533,"end":536},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T4","span":{"begin":1412,"end":1415},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T5","span":{"begin":1479,"end":1482},"obj":"http://purl.obolibrary.org/obo/GO_0005790"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":104,"end":121},"obj":"http://purl.obolibrary.org/obo/UBERON_0002384"},{"id":"T2","span":{"begin":264,"end":281},"obj":"http://purl.obolibrary.org/obo/UBERON_0002384"},{"id":"T3","span":{"begin":115,"end":121},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T4","span":{"begin":275,"end":281},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":104,"end":121},"obj":"http://purl.obolibrary.org/obo/MAT_0000301"},{"id":"T2","span":{"begin":264,"end":281},"obj":"http://purl.obolibrary.org/obo/MAT_0000301"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":115,"end":121},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":275,"end":281},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":104,"end":121},"obj":"http://purl.obolibrary.org/obo/UBERON_0002384"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":264,"end":281},"obj":"http://purl.obolibrary.org/obo/UBERON_0002384"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":104,"end":121},"obj":"Body_part"},{"id":"T2","span":{"begin":264,"end":281},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000301"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000301"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":104,"end":121},"obj":"Body_part"},{"id":"T2","span":{"begin":264,"end":281},"obj":"Body_part"},{"id":"T3","span":{"begin":1532,"end":1540},"obj":"Body_part"},{"id":"T4","span":{"begin":1776,"end":1784},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002384"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002384"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"}],"text":"NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.\nComplete 1H and 13C NMR assignments are reported for two glycopeptides representing the carbohydrate-protein linkage region of connective tissue proteoglycans. These glycopeptides are the octasaccharide hexapeptide, Ser(GlcpAbeta(1--\u003e3) Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylpbeta)-Gly-Ser-Gly-Se r (GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)Xylp beta)-Gly (1), and the tetrasaccharide dipeptide, Ser(GlcpAbeta(1--\u003e3)Galpbeta(1--\u003e3)Galpbeta(1--\u003e4)X ylpbeta)-Gly (2). The vicinal coupling constant data show that the monosaccharide residues adopt4 C 1 chair conformations. 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. 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--\u003e3) linkage, +ac for beta(1--\u003e4) linkage). The predominant conformation about the glycopeptide bond is straight phi = -sc and psi = +ac. 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. 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."}