Fidelity Mechanisms of the Aminoacyl-tRNA Synthetases View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2009

AUTHORS

A. P. Mascarenhas , S. An , A. E. Rosen , S. A. Martinis , K. Musier-Forsyth

ABSTRACT

The central dogma and its accurate interpretation by a large array of biomolecules remains a fascinating process. Understanding its mechanisms of decoding holds tremendous potential for the future of protein engineering. The family of aminoacyl transfer RNA (tRNA) synthetases (AARSs) is at the forefront of this field. While aminoacylation is the primary role of these enzymes, they possess various additional functions that are important to cell survival. An editing activity, which clears incorrectly attached amino acids, minimizes errors in protein synthesis. If this error correction mechanism is disabled, the incorporation of novel amino acids into proteins offers an exciting approach to expand the genetic code (Döring et al. 2001; Nangle et al. 2006). This chapter focuses on the AARSs that have amino acid editing functions with an emphasis on their continuing dynamic role in the field of protein engineering. More... »

PAGES

155-203

References to SciGraph publications

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  • Book

    TITLE

    Protein Engineering

    ISBN

    978-3-540-70937-4
    978-3-540-70941-1

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/978-3-540-70941-1_6

    DOI

    http://dx.doi.org/10.1007/978-3-540-70941-1_6

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1009115580


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