Glycoproteomics: The sweet smell ofwe’re-getting-there
The Jan. 7 issue of
Science magazine includes my latest Life
Science Technologies feature, on glycoproteomics.
Concentrating on the sweet science of mass spectrometry, this
article examines the technical challenges inherent in cataloging
and characterizing all the carbohydrate modifications on all the
proteins in a given cell, tissue, or organism.
Some 50 percent of eukaryotic proteins, and not just those
on the cell surface, are dusted with sugars like some molecular
pastry. These glycan modifications can assume a seemingly limitless
array of forms, compositions, and chemical linkages. Complicating
matters, any given protein location may contain dozens of subtly
different sugars (other modifications, like phosphorylation, are
more binary — they are either there, or they’re not). The
resulting structural heterogeneity poses a serious challenge to the
researchers who would study them, and in the past, their solution
has largely been to punt: Glycomicists studied sugars, and
proteomicists studied proteins, and ne’er the twain shall meet.
But, as a growing body of research shows, some researchers are
bucking that trend, albeit slowly. Witness the painstaking and
laborious characterization of just a single protein,
alpha-dystroglycan.
Glycoproteomics, says James Paulson,
principal investigator of the Consortium for Functional
Glycomics, “is becoming
mainstream.”
Biotechnically Speaking 