Related ArticlesNMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.
Glycobiology. 1999 Jul;9(7):669-77
Authors: Agrawal PK, Jacquinet JC, Krishna NR
Complete 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-->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). 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-->3) linkage, +ac for beta(1-->4) 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.
[NMR paper] NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimen
NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.
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Chembiochem. 2004 Sep 6;5(9):1245-55
Authors: Aboitiz N, Vila-Perelló M, Groves P, Asensio JL, Andreu D, Cañada FJ, Jiménez-Barbero...
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[NMR paper] NMR and molecular modeling studies of the interaction between wheat germ agglutinin a
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Biochemistry. 2004 Aug 3;43(30):9647-54
Authors: Lycknert K, Edblad M, Imberty A, Widmalm G
The beta-D-GlcpNAc-(1-->6)-alpha-D-Manp disaccharide is a constituent of highly...
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[NMR paper] NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-
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Carbohydr Res. 2004 Apr 2;339(5):907-28
Authors: Johnson MA, Pinto BM
Investigations of the conformations of carbohydrates, their analogues and their molecular mimics are described, with emphasis on structural and functional information that can be gained by NMR spectroscopic techniques in combination with molecular...
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[NMR paper] NMR and molecular modeling of complex carbohydrates and carbohydrate-protein interact
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Adv Exp Med Biol. 2001;491:543-50
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In order to characterize the conformational epitope of the group B meningococcal polysaccharide and of the type III group B Streptococcus capsular polysaccharide NMR measurements were done on a wide...
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[NMR paper] A mini-protein designed by removing a module from barnase: molecular modeling and NMR
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Protein Eng. 1999 Aug;12(8):673-80
Authors: Takahashi K, Noguti T, Hojo H, Yamauchi K, Kinoshita M, Aimoto S, Ohkubo T, G? M
A globular domain can be decomposed into compact modules consisting of contiguous 10-30 amino acid residues. The correlation between modules and exons observed in...
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Glycoconj J. 1996 Aug;13(4):599-607
Authors: Curto EV, Sakai TT, Jablonsky MJ, Rio-Anneheim S, Jacquinet JC, Krishna NR
We present complete 1H NMR assignments for two synthetic glycopeptides representative of the carbohydrate-protein linkage region of serglycin proteoglycans. The peptides are:...
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Biochemistry. 1991 Jun 18;30(24):5851-7
Authors: McManus S, Riechmann L
Two-dimensional (2D) 1H NMR spectroscopy was used to study the hapten-binding site of a recombinant antibody Fv fragment expressed in Escherichia coli. Point mutations...
NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein
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