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Glycomics, an analogous term to genomics and proteomics, is the comprehensive study of glycomes (the entire complement of sugars, whether free or present in more complex molecules, of an organism), including genetic, physiologic, pathologic, and other aspects.[1][2] Glycomics "is the systematic study of all glycan structures of a given cell type or organism" and is a subset of glycobiology.[3] The term glycomics is derived from the chemical prefix for sweetness or a sugar, "glyco-", and was formed to follow the naming convention established by genomics (which deals with genes) and proteomics (which deals with proteins).
[edit] Challenges
This area of research has to deal with an inherent level of complexity not seen in other areas of applied biology. 68 building blocks (molecules for DNA, RNA and proteins; categories for lipids; types of sugar linkages for saccharides) provide the structural basis for the molecular choreography that constitutes the entire life of a cell. DNA and RNA have four building blocks each (the nucleosides or nucleotides). Lipids are divided into eight categories based on ketoacyl and isoprene. Proteins have 20 (the amino acids). Saccharides have 32 types of sugar linkages.[4]. While these building blocks can be attached only linearly for proteins and genes, they can be arranged in a branched array for saccharides, further increasing the degree of complexity. [edit] ImportanceTo answer of this question one should know the different and important functions of glycans. The following are some of those functions:
[edit] Tools usedThe following are examples of the commonly used techniques in glycan analysis [5] [edit] High Resolution Mass SpectrometryThe most applied method in which the glycan part of a glycoprotein is separated from the protein and subjected to analysis by multiple rounds of mass spectrometry. In case of glycolipids, they can be analyzed directly without separation of the lipid component. Mass spectrometry can be used in conjunction with HPLC.
[edit] Lectin and Antibody ArrayIt provides high-throughput screening of many samples containing glycans. This method uses either naturally occurring lectins or artificial monoclonal antibodies, where both are immobilized on a certain chip and incubated with a fluorescent glycoprotein sample. [edit] Metabolic and covalent labeling of glycansMetabolic labeling of glycans can be used as a way to detect glycan structures. A well known strategy involves the use of azide-labeled sugars which can be reacted using the Staudinger ligation. This method has been used for in vitro and in vivo imaging of glycans. [edit] See also
[edit] References
[edit] External links
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