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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Main Authors: Serge Pérez, Daniele de Sanctis
Format: Article
Language:English
Published: Beilstein-Institut 2017-06-01
Series:Beilstein Journal of Organic Chemistry
Subjects:
Online Access:https://doi.org/10.3762/bjoc.13.114
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spelling 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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