ORGN 666 |
| Phosphorylation, a ubiquitous protein post-translational modification in cells, is involved in a multitude of cellular functions ranging from protein synthesis, muscular contraction, and cellular division. With phosphorylation playing a major role in cell function, characterization of phosphoproteins as well as the kinases catalyzing phosphorylation is important. We have recently discovered that kinases display cofactor promiscuity, accepting γ-phosphate modified ATP-derivatives for phosphorylation of full-length proteins. Utilizing the promiscuity of kinases, we envision creating various ATP derivatives for phosphoprotein identification, phosphoprotein purification and development of phosphorylation assays. Specifically, we have used an ATP-biotin conjugate that allowed kinase-catalyzed biotin tagging of phosphoproteins for subsequent detection. Because kinase-catalyzed protein tagging is compatible with natural substrates and enzymes in native conditions, it holds promise for being a thrilling new tool in phosphoproteomics and signaling transduction research.
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Asymmetric Reactions, Combinatorial Chemistry, Molecular Recognition and Self-Assembly, Proteins, Peptides, Amino Acids and Enzyme Inhibitors
8:00 PM-10:00 PM, Wednesday, March 28, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Sci-Mix
Division of Organic Chemistry |
