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    Use of Geometrical Docking Algorithm to Explore Species Specific Differences in Proyl-tRNA Synthetases

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    TheisenSpr17.pdf (2.778Mb)
    TheisenSpr17.pptx (4.530Mb)
    Date
    2018-02-08
    Author
    Bhattacharyya, Sudeep
    Theisen, Cole
    Reinhardt, Clorice R.
    Metadata
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    Abstract
    Prolyl-tRNA synthetases belong to a class of enzymes that play a pivotal role in the protein synthesis. These enzymes are responsible for attaching the amino acid, proline, to the 3’ end of the prolyl-tRNA. The structures and domain architectures of these enzymes differ considerably between human and their pathogenic analogs. Identifying the differences of recognition elements present in the two active sites can lead to selective inhibitors based on structure. In the present study, computer-aided docking and simulations have been carried out on several substrate (proline) and inhibitor (halofuginone) analogs.
    Subject
    Proyl-tRNA synthetases
    Chemistry
    Enzymes
    Posters
    Permanent Link
    http://digital.library.wisc.edu/1793/77969
    Description
    Color poster with text, models, and images.
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    • Student Research Day

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