Riley, Nicholas M.; Hebert, Alexander S.; Westphall, Michael S.; Coon, Joshua J. published the artcile< Capturing site-specific heterogeneity with large-scale N-glycoproteome analysis>, Synthetic Route of 3458-28-4, the main research area is glycoproteome glycopeptide IR photon ion electron transfer dissociation.
Protein glycosylation is a highly important, yet poorly understood protein post-translational modification. Thousands of possible glycan structures and compositions create potential for tremendous site heterogeneity. A lack of suitable anal. methods for large-scale analyses of intact glycopeptides has limited our abilities both to address the degree of heterogeneity across the glycoproteome and to understand how this contributes biol. to complex systems. Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue. Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein. Moreover, we use this large-scale glycoproteomic dataset to develop several visualizations that will prove useful for analyzing intact glycopeptides in future studies.
Nature Communications published new progress about Animal gene, Sparc Role: ANT (Analyte), BSU (Biological Study, Unclassified), ANST (Analytical Study), BIOL (Biological Study). 3458-28-4 belongs to class alcohols-buliding-blocks, and the molecular formula is C6H12O6, Synthetic Route of 3458-28-4.
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts