| TECHNOLOGY |
One of the major complications of analyzing proteomes is that a lot of proteins are glycosylated. Glycosylated proteins participate in a multitude of biochemical interactions and play an important role in immunity and disease, but researchers "are only at the beginning of understanding the physiological functions of glycoproteins," he said. Having the ability to analyze the structures of oligosaccharide groups on glycosylated proteins would help, but it remains a tremendous challenge. Glycosylated proteins are enormously complex, each type is typically present in cells in vanishingly small amounts, and no technique like polymerase chain reaction (used to amplify DNA) is available to amplify them. "Analytical chemistry advances will be needed to address this problem. "There's a need for new instrumentation that is faster and more informative."
He and his coworkers are developing microscale enzymatic cleavage procedures to remove oligosaccharides from glycosylated proteins and novel capillary electrochromatography (CEC) media to separate the cleaved sugar groups
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