Development of a Synthetic Receptor for Pyrophosphorylated Proteins

Author/​Artist
Rakonjac, Nevena [Browse]
Format
Senior thesis
Language
English
Description
76 pages

Availability

Available Online

Copies in the Library

Location Call Number Status Location Service Notes
Mudd Manuscript Library - StacksAC102 Browse related items On-site accessReading Room Request

    Details

    Advisor(s)
    Fiedler, Dorothea [Browse]
    Department
    Princeton University. Department of Chemistry [Browse]
    Class year
    2013
    Restrictions note
    Walk-in Access. This thesis can only be viewed on computer terminals at the Mudd Manuscript Library.
    Summary note
    Pyrophosphoinositol polyphosphates (PP-IPs) are considered to have an important role in intracellular signaling and adaptation to environmental factors and stress. Although not fully understood, they are postulated to function by two distinct mechanisms: binding to proteins allosterically affecting them, or by pyrophosphorylating pre-phosphorylated proteins in a non-enzymatic fashion. The latter has been observed only in vitro due to the lack of methods to study and identify pyrophosphorylated proteins in vivo. The overarching purpose of this project is to create an affinity reagent that will selectively bind to pyrophosphorylated proteins in cell lysates. The affinity reagents examined were tested for selective binding of a pyrophosphorylated protein mimic, UDP.
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    Supplementary Information