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  • A theoretical study to establish the relationship between the three-dimensional structure of triose-phosphate isomerase of Giardia duodenalis and point mutations in the respective gene

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    Author(s)
    Nolan, Matthew J
    Hofmann, Andreas
    Jex, Aaron R
    Gasser, Robin B
    Griffith University Author(s)
    Hofmann, Andreas
    Year published
    2010
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    Abstract
    Predicting how point mutations in genes alter the tertiary and quarternary structure of proteins is central to a number of areas of molecular biology and has implications in relation to the function and evolution of molecules. In the present study, we theoretically assessed the effects of 20 point mutations detected previously in a region of the triose-phosphate isomerase gene (tpi) of the protozoan Giardia duodenalis on the three-dimensional structure of the 'wild-type' protein (TPI). Amino acid substitutions arising from codon variations were mainly located at surface-accessible sites or in hydrophobic pockets of TPI. None ...
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    Predicting how point mutations in genes alter the tertiary and quarternary structure of proteins is central to a number of areas of molecular biology and has implications in relation to the function and evolution of molecules. In the present study, we theoretically assessed the effects of 20 point mutations detected previously in a region of the triose-phosphate isomerase gene (tpi) of the protozoan Giardia duodenalis on the three-dimensional structure of the 'wild-type' protein (TPI). Amino acid substitutions arising from codon variations were mainly located at surface-accessible sites or in hydrophobic pockets of TPI. None of the substitutions was predicted to exert a significant change to the fold or functionality of the enzyme, with the exception of one alteration (Arg100). Almost all substitutions were either conservative or semi-conservative, and retained or even improved the expected stability of the fold. Overall, the findings provide support for the "neutral theory", which contends that evolution at the molecular level is not solely shaped by "Darwinian selection but also by random drift of selectively neutral or nearly neutral mutants".
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    Journal Title
    Molecular and Cellular Probes
    Volume
    24
    Issue
    5
    DOI
    https://doi.org/10.1016/j.mcp.2010.06.001
    Copyright Statement
    © 2010 Elsevier. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
    Subject
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Structural biology (incl. macromolecular modelling)
    Publication URI
    http://hdl.handle.net/10072/34038
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    • Journal articles

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