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Development of a Synthetic Receptor for Pyrophosphorylated Proteins
Author/Artist
Rakonjac, Nevena
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Format
Senior thesis
Language
English
Description
76 pages
Availability
Available Online
Citation only:
DataSpace
Copies in the Library
Location
Call Number
Status
Location Service
Notes
Mudd Manuscript Library - Stacks
AC102
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Details
Advisor(s)
Fiedler, Dorothea
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Department
Princeton University. Department of Chemistry
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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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