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Special focus on glycomics in OMICS: A Journal of Integrative Biology
Date:9/10/2010

structures that differ in the nine-carbon sugars that comprise their backbone, how they are attached and arranged on the cell membrane, and their overall structure. In the article, "Proteoglycomics: Recent Progress and Future Challenges," Mellisa Ly, Tatiana Laremore, and Robert Linhardt, from Rensselaer Polytechnic Institute (Troy, NY), describe the unique challenges involved in characterizing the composition, structure, and structure-function relationships of proteoglycans, which are comprised of core proteins modified through the attachment of varied sugar structures.

"Although glycomics may still be a frontier omics field, we believe that it has a bright future in the postgenome era," says Jeremy Turnbull. "Glycosylation of biomolecules alters their biological function and, in some cases, the glycans themselves have intrinsic and independent functions. This affords diverse opportunities for subtle regulation of biological processes at a higher level of complexity than DNA or proteins."


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Contact: Vicki Cohn
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Mary Ann Liebert, Inc./Genetic Engineering News
Source:Eurekalert

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