ORGN 709 |
| The phosphorylation state of specific side chains in signal proteins controls the activation and termination of a host of cellular processes. Phosphatase enzymes are responsible for hydrolytic removal of Pi from proteins, corresponding to an “off” signal. Enzyme activity typically varies with the ionic composition of the medium; we are interested in further tuning such activity by appending ion-sensitive moieties (i.e., crown ethers) to model systems for phosphotyrosine (pTyr). Using protein tyrosine phosphatase from Yersinia, we find that dephosphorylation is inhibited when an alkali metal ion is bound within the crown.
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Asymmetric Reactions, Molecular Recognition, Self Assembly, Bioorganic Chemistry, Process R&D
8:00 PM-10:00 PM, Wednesday, 16 March 2005 Convention Center -- Hall D, Poster
Division of Organic Chemistry |
