Abstract
Oligosaccharide chains often constitute a large proportion of the molecular mass of glycoproteins. Their relative hydrophilicity, flexibility and heterogeneity can make crystallisation difficult or impossible for X-ray studies of the native molecule and hence NMR spectroscopy is the method of choice for analysis. NMR is also useful for analysis of oligosaccharide sequences found on glycoproteins, glycolipids, proteoglycans, polysaccharides, antibiotics and as free oligosaccharides which are recognition determinants and potential drugs. Their multiple chiral centres and polyhydroxyl functionality make oligosaccharides important natural information molecules and artificial templates on which to stereochemically design ligands for different protein or DNA binding motifs.
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References
Coombe DR, Harrop HA, Hounsell EF, Bauer CJ, Feeney J, Mahmood N, Mulloy B, Parish CR and Rider CC (submitted) The anti-HIV-1 activity of chemically modified heparins: correlation between GP-120 V3 loop binding and inhibition of cellular HIV-1 infection in vitro. Biochemistry
Desai UR, Wang HM, Kelly TR and Linhardt RJ (1992) Structure elucidation of a novel acidic tetrasaccharide and hexasaccharide derived from a chemically modified heparin. Carbohydr. Res. 241: 249–259
Feeney J, Frenkiel TA and Hounsell EF (1986) Complete XH-N.M.R. assignments for two core-region oligosaccharides of human meconium glycoproteins, using ID and 2D methods at 500 MHz. Carbohydr. Res. 152: (1986) 63–72
Gettins P and Home AP (1992) One- and two-dimensional 13c-n. m. r. characterization of two series of oligosaccharides derived from porcine intestinal mucosal heparin by degradation with heparinase. Carbohydr. Res. 223: 81–98
Gooi HC, Picard JK, Hounsell EF, Gregoriou M, Rees AR and Feizi T (1985a) Monoclonal antibody (EGR/G49) reactive with the epidermal growth factor receptor of A431 cells recognizes the blood group ALeto and ALeY structures. Mol. Immunol. 22: 689–693
Gooi HC, Hounsell EF, Lax I, Kris RM, Libermann TA, Schlessinger J, Sato JD, Kawamato T, Mendelsohn J and Feizi T (1985b) The carbohydrate sepcificities of the monoclonal antibodies 29.1, 455 and 3C1B12 to the epidermal growth factor receptor of A431 cells. Biosci. Rep. 5: 83–94
Home A and Gettins P (1991) XH-N. m. r. spectral assignments for two series of heparin-derived oligosaccharides. Carbohydr. Res. 225: 43–57
Hounsell EF, Lawson AM, Feeney J, Gooi HC, Pickering NJ, Stoll MS, Lui SC and Feizi T (1985) Structural analysis of the O-glycosidically linked core-region oligosaccharides of human meconium glycoproteins which express oncofoetal antigens. Eur. J. Biochem. 148: 367–377
Hounsell EF, Feeney J, Scudder P, Tang PW and Feizi T (1986) XH-NMR studies at 500 MHz of a neutral disaccharide and sulphated di-, tetra-, hexa- and larger oligosaccharides obtained by endo-B-galactosidase treatment of keratan sulphate. Eur. J. Biochem. 157: 375–384
Hounsell EF (1987) Structural and conformational characterization of carbohydrate differentiation antigens. Chem. Soc. Rev. 16: 161–185
Hounsell EF, Jones NJ, Gooi HC and Feizi T (1988) 500-MHz XH-N.M.R. and conformational studies of fucosyloligosaccharides recognised by monoclonal antibodies with specificities related to Lea, Leto, and SSEA-1. Carbohydr. Res. 178: 67–78
Hounsell EF and Wright DJ (1990) Computer-assisted interpretation of xH-n. m. r. spectra in the analysis fo the structure of oligosaccharides. Carbohydr. Res. 205: 19–29
Hounsell EF and Davies MJ (1993) Role of protein glycosylation in immune regulation. Ann. Rheum. Dis. 52: S22-S29
Hounsell EF (1993) A general strategy for glycoprotein oligosaccharide analysis. In EF Hounsell ed. Methods in Molecular Biology Vol 14 Glycoprotein Analysis in Biomedicine, Humana Press Ch1
Linhardt RJ, Rice KG, Merchant ZM, Kim YS and Lohse DL (1986) Structure and activity of a unique heparin-derived hexasaccharide. J. Biol. Chem. 261: 1448–14454
Linhardt RJ, Wang HM, Loganathan D, and Bae JH (1992) Search for the heparin antithorombin Ill-binding site precursor. J. Biol. Chem. 267: 2380–2387
Petitou M, Lormeau JC, Perly B, Berthault P, Bossennec V, Sie P and Choay J (1988) Is there a unique sequence in heparin for interaction with heparin cofactor II? Structural and biological studies of heparin-derived oligosaccharides. J. Biol. Chem. 263: 8865–8690
Smith KD, Davies MJ and Hounsell EF (1994) Structural profiling of oligosaccharides. In J. Walker ed. Methods in Molecular Biology Vol 20 Protocols for Proteins and Peptides Humana Press Ch18
Smith KD, Davies MJ, Carruthers RA, Cashmore GC, Purkiss P, Lawson AM and Hounsell EF (Submitted) Analysis of the glycosylation patterns of the extracellular domain of the receptor for epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts. Anal. Biochem.
Renouf DV and Hounsell EF (1992) Conformational studies of the backbone (poly-N-acetyllactosamine) and the core region sequences of O-linked carbohydrate chains. Int. J. Biol. Macromol 15: 37–42
Yamada S, Yoshida K, Sugiura M, Sugahara K, Khoo K, Morris HR and Dell A (1992) Structural studies on the bacterial lyase-resistant tetrasaccharides derived from the antithrombin Ill-binding site of procine intesstinal heparin. J. Biol. Chem. 268: 4780–4787
van Boeckel CA, Grootenhuis PD, and Haasnoot CA (1991) Specificity in the recognition process between charged carbohydrates and proteins. Trends. Pharmacol. Sci. 12: 241–243
van Kuik JA, Hard K and Vliegenthart JFG (1992) A XH NMR database computer program for the analysis of the primary structure of complex carbohydrates. Carbohyd. Res. 235: 63–68
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© 1994 Springer-Verlag Berlin Heidelberg
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Hounsell, E.F. (1994). Structural and Conformational Studies of Glycoproteins and Oligosaccharide Recognition Determinants. In: Stassinopoulou, C.I. (eds) NMR of Biological Macromolecules. NATO ASI Series, vol 87. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79158-1_13
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DOI: https://doi.org/10.1007/978-3-642-79158-1_13
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