Princeton University Library Catalog

Development of a Synthetic Receptor for Pyrophosphorylated Proteins

Rakonjac, Nevena [Browse]
Senior thesis
Fiedler, Dorothea [Browse]
Princeton University. Department of Chemistry [Browse]
Class year:
76 pages
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.