By Steffen B. Petersen, Birte Svensson and Sven Pedersen (Eds.)
The Carbohydrate Bioengineering assembly held in Elsinore, Denmark, April 23-26, 1995, amassed 230 scientists, normally from Europe, with curiosity in carbohydrate research and constitution; carbohydrates in medication and glycopathology; constitution, functionality, software, and protein engineering of carbohydrate energetic enzymes; oligo- and polysaccharides of business curiosity; and construction of carbohydrate containing new materials.
The first chapters tackle glycoconjugates as modulatory and popularity molecules, constitution decision utilizing NMR and mass spectrometry, and microdialysis-chip enzyme-based sensors. lively web site mutations coupled with crystal constructions and artificial substrate analogue interactions in addition to new three-d buildings and binding domain names for biotechnological purposes are incorporated within the chapters. Carbohydrate energetic enzymes became out to be a foremost topic.
The swift improvement in glycobiology and glycotechnology has led to an incredible elevate in our wisdom at the constitution conversion, and alertness of carbohydrates in and medication.
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Additional resources for Carbohydrate Bioengineering, Proceedings of an International Conference
HOI ~ 0 1C H2 5 C H20H 6 In this study we refine our investigations of sucrose at low temperatures in aqueous solutions in an effort to shed light on the existence of any interresidue hydrogen bonds in the context of its newly revealed flexibility around the glycosidic bond. We were aware that a great deal of effort had been spent by others [27,28] examining intramolecular hydrogen bonding and determining its effect on the overall conformation of sucrose in solution. However, we are the first to use the hydroxyl proton signals of sucrose in supercooled aqueous solution as NMR probes for the detection of intramolecular hydrogen bonds.
IIo/, o, ~'CHDOMe ~J I / J' ~ P "" "~_j~'MeOCHD / Iu\ ~ i MeODHC' I " MeO CH2OMe~ ] o J ~ 378 MeOOC O / I 257 ~-- 289 MOeocHD l 874 4--906 o e 233 ~ Hoh o ~MeOL~ MeODHC r I (453) O. e N ~Ac 478 J--'--CH2OMe j CHOMe MeODHC ==m=~If~,JrO --CH2 CHrOMe O 7a. . . . . 0h. . . . . sa. . . . i0'D8 CH2OMe"~ MeNAc I - CH'~ 874 906 m/z 666 ~ - 698 MeOOC---] f- CH-~2 ~ CHDOM. 666 Low mass scan 257 4-- 289 >800 x3 I ii i ~L~ Me. m/z 698 196 2g. Ac/ [M+23]* OO M ~ ~ O T ' ~H I CHDOMe MeNAc I M e O D H C ==~====If "I"*O 666 ~-- 698 874 ~-- 906 Figure 6.
GBF Monographs 15 (1990) 125. Copyright 1995 VCH. giving other sequence ions than the above. No sequence ion corresponding to cleavage of the oxidised Gal residue, which would be m/z 453 is seen, instead an ion of m/z 378 is formed by cleavage of the carbon 5 and the former ring oxygen bond of the periodate degraded Gal residue. Both antennae of this biantennary structure contain 2-6 sialylated sequences. These sequences are linked to the 2-position of a mannose residue, deduced from the primary and secondary ions of m/z 906 and m/z 874, respectively.