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    • University of Missouri-Columbia
    • Graduate Studies - Theses and Dissertations (MU)
    • Theses and Dissertations (MU)
    • Dissertations (MU)
    • 2015 Dissertations (MU)
    • 2015 MU dissertations - Freely available online
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    Kinetics and mechanisms associated with redox regulation of protein tyrosine phosphatase 1B (PTP1B)

    Parsons, Zachary D.
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    Date
    2015
    Format
    Thesis
    Metadata
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    Abstract
    Here, we report on the kinetics and mechanisms associated with redox regulation of the protein tyrosine phosphatase PTP1B. We determined rates of thiol- and phosphinemediated recovery of catalytic activity from the oxidatively-inactivated enzyme, and shed light on the chemical mechanisms involved in these processes and in the regulation of PTP family member SHP2. Additionally, we describe reactions that oxidatively-inactivated PTP1B undergo with structurally-diverse carbon acids, using both a small chemical model dipeptide of oxidatively-inactivated PTP1B, and the oxidized enzyme itself. Finally, we report a novel method by which to predict Hammett substituent constants via electronic structure calculations.
    URI
    https://hdl.handle.net/10355/49109
    Degree
    Ph. D.
    Thesis Department
    Chemistry (MU)
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    • 2015 MU dissertations - Freely available online
    • Chemistry electronic theses and dissertations (MU)

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