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A systematic approach to protein glycosylation analysis: a path through the maze

A systematic approach to protein glycosylation analysis: a path through the maze Protein glycosylation is an important post-translational modification. It is a feature that enhances the functional diversity of proteins and influences their biological activity. A wide range of functions for glycans have been described, from structural roles to participation in molecular trafficking, self-recognition and clearance. Understanding the basis of these functions is challenging because the biosynthetic machinery that constructs glycans executes sequential and competitive steps that result in a mixture of glycosylated variants (glycoforms) for each glycoprotein. Additionally, naturally occurring glycoproteins are often present at low levels, putting pressure on the sensitivity of the analytical technologies. No universal method for the rapid and reliable identification of glycan structure is currently available; hence, research goals must dictate the best method or combination of methods. To this end, we introduce some of the major technologies routinely used for structural N- and O-glycan analysis, describing the complementary information that each provides. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Chemical Biology Springer Journals

A systematic approach to protein glycosylation analysis: a path through the maze

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References (95)

Publisher
Springer Journals
Copyright
Copyright © 2010 by Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
Subject
Chemistry; Chemistry/Food Science, general; Biochemical Engineering; Biochemistry, general; Cell Biology; Bioorganic Chemistry
ISSN
1552-4450
eISSN
1552-4469
DOI
10.1038/nchembio.437
Publisher site
See Article on Publisher Site

Abstract

Protein glycosylation is an important post-translational modification. It is a feature that enhances the functional diversity of proteins and influences their biological activity. A wide range of functions for glycans have been described, from structural roles to participation in molecular trafficking, self-recognition and clearance. Understanding the basis of these functions is challenging because the biosynthetic machinery that constructs glycans executes sequential and competitive steps that result in a mixture of glycosylated variants (glycoforms) for each glycoprotein. Additionally, naturally occurring glycoproteins are often present at low levels, putting pressure on the sensitivity of the analytical technologies. No universal method for the rapid and reliable identification of glycan structure is currently available; hence, research goals must dictate the best method or combination of methods. To this end, we introduce some of the major technologies routinely used for structural N- and O-glycan analysis, describing the complementary information that each provides.

Journal

Nature Chemical BiologySpringer Journals

Published: Sep 17, 2010

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