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    Domain-Domain Communication for tRNA Aminoacylation : Importance of Evolutionarily Conserved and Energetically Coupled Residues.

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    File(s)
    ShaneSpr08.pdf (1.461Mb)
    ShaneSpr08.pptx (8.086Mb)
    Date
    2009-02-10
    Author
    Weimer, Kristina
    Shane, Brianne
    Advisor(s)
    Hati, Sanchita
    Metadata
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    Abstract
    Aminoacyl tRNA synthetases (ARSs) are an important family of protein enzymes that play a key role in protein biosynthesis. ARSs catalyze the covalent attachment of amino acids to their cognate transfer RNA (tRNA). In the present work, we investigated the molecular basis of long-range domain-domain communication in Escherichia coliprolyl-tRNA synthetase (E. coli ProRS).
    Subject
    RNA
    Aminocyl-tRNA synthetases
    RNA-protein interactions
    Proteins--Synthesis
    Posters
    Permanent Link
    http://digital.library.wisc.edu/1793/32224
    Description
    Color poster with text and images describing research conducted by Brianne Shane and Kristina Weimer, advised by Sanchita Hati.
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    • Student Research Day

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