Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience
Synchrotron radiation is the most versatile way to explore biological materials in different states: monocrystalline, polycrystalline, solution, colloids and multiscale architectures. Steady improvements in instrumentation have made synchrotrons the most flexible intense X-ray source. The wide range...
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doaj-ed572029783c43f38d8bf8c787e4b9872021-04-02T10:09:35ZengBeilstein-InstitutBeilstein Journal of Organic Chemistry1860-53972017-06-011311145116710.3762/bjoc.13.1141860-5397-13-114Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscienceSerge Pérez0Daniele de Sanctis1Department of Molecular Pharmacochemistry, CNRS-University Grenoble Alpes, FranceESRF – The European Synchrotron, Grenoble, FranceSynchrotron radiation is the most versatile way to explore biological materials in different states: monocrystalline, polycrystalline, solution, colloids and multiscale architectures. Steady improvements in instrumentation have made synchrotrons the most flexible intense X-ray source. The wide range of applications of synchrotron radiation is commensurate with the structural diversity and complexity of the molecules and macromolecules that form the collection of substrates investigated by glycoscience. The present review illustrates how synchrotron-based experiments have contributed to our understanding in the field of structural glycobiology. Structural characterization of protein–carbohydrate interactions of the families of most glycan-interacting proteins (including glycosyl transferases and hydrolases, lectins, antibodies and GAG-binding proteins) are presented. Examples concerned with glycolipids and colloids are also covered as well as some dealing with the structures and multiscale architectures of polysaccharides. Insights into the kinetics of catalytic events observed in the crystalline state are also presented as well as some aspects of structure determination of protein in solution.https://doi.org/10.3762/bjoc.13.114antibodiescarbohydrate binding domainscelluloseglycosaminoglycansglycolipidsglycosyl hydrolasesglycosyl transferaseskinetic crystallographylectinspolysaccharidespowder diffractionsmall-angle X-ray scatteringstarchsynchrotron radiationtransportersX-ray crystallography |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Serge Pérez Daniele de Sanctis |
spellingShingle |
Serge Pérez Daniele de Sanctis Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience Beilstein Journal of Organic Chemistry antibodies carbohydrate binding domains cellulose glycosaminoglycans glycolipids glycosyl hydrolases glycosyl transferases kinetic crystallography lectins polysaccharides powder diffraction small-angle X-ray scattering starch synchrotron radiation transporters X-ray crystallography |
author_facet |
Serge Pérez Daniele de Sanctis |
author_sort |
Serge Pérez |
title |
Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience |
title_short |
Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience |
title_full |
Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience |
title_fullStr |
Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience |
title_full_unstemmed |
Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience |
title_sort |
glycoscience@synchrotron: synchrotron radiation applied to structural glycoscience |
publisher |
Beilstein-Institut |
series |
Beilstein Journal of Organic Chemistry |
issn |
1860-5397 |
publishDate |
2017-06-01 |
description |
Synchrotron radiation is the most versatile way to explore biological materials in different states: monocrystalline, polycrystalline, solution, colloids and multiscale architectures. Steady improvements in instrumentation have made synchrotrons the most flexible intense X-ray source. The wide range of applications of synchrotron radiation is commensurate with the structural diversity and complexity of the molecules and macromolecules that form the collection of substrates investigated by glycoscience. The present review illustrates how synchrotron-based experiments have contributed to our understanding in the field of structural glycobiology. Structural characterization of protein–carbohydrate interactions of the families of most glycan-interacting proteins (including glycosyl transferases and hydrolases, lectins, antibodies and GAG-binding proteins) are presented. Examples concerned with glycolipids and colloids are also covered as well as some dealing with the structures and multiscale architectures of polysaccharides. Insights into the kinetics of catalytic events observed in the crystalline state are also presented as well as some aspects of structure determination of protein in solution. |
topic |
antibodies carbohydrate binding domains cellulose glycosaminoglycans glycolipids glycosyl hydrolases glycosyl transferases kinetic crystallography lectins polysaccharides powder diffraction small-angle X-ray scattering starch synchrotron radiation transporters X-ray crystallography |
url |
https://doi.org/10.3762/bjoc.13.114 |
work_keys_str_mv |
AT sergeperez glycosciencesynchrotronsynchrotronradiationappliedtostructuralglycoscience AT danieledesanctis glycosciencesynchrotronsynchrotronradiationappliedtostructuralglycoscience |
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1724167898435420160 |