Glycosylation is
the most abundant post-translational modification of proteins. Estimates vary
widely, but a common assessment is that upwards of 50% of eukaryotic proteins
are modified by some type of glycan. Indeed, the difficulties associated with
accurately assessing the glycosylation status of intra- and extracellular
proteins are the primary motivations for this volume. Over the past 30 years,
insight into the biological roles of glycan modifications has grown
dramatically, yet this field has often struggled due to the inadequacies of
accessible analytical methods. Fortunately, simultaneous to the recent
expansion of knowledge in glycobiology, a similar transformation has occurred
in the field of glycoproteomics. New enrichment techniques, novel ionization
methods, mass spectrometry technologies, the expanding role of high-performance
liquid chromatography, and improved informatics resources have transformed
niche characterization of discrete glycoproteins into a powerful “omics”
toolset that can simultaneously characterize diverse glycoproteins and the Glycans
they carry. Although proteomics approaches have been applied to broad classes
of posttranslational modifications, glycoproteins represent a particularly
challenging case due to the heterogeneity of glycan structures, the lability of
glycosidic bonds, the isobaric nature of many monosaccharides, and the difficulties
associated with determining the unique structure of a branched molecule from
compositional analysis. As presented in this volume, the latest glycoproteomics
tools are meeting these challenges, providing unprecedented information about
the structure and diversity of glycoproteins. It is an exciting time to be both
a glycobiologist and mass spectrometrist.
0 comments:
Post a Comment