Type
Text
Type
Thesis
Advisor
French, Jarrod B | Kaczocha, Martin.
Date
2014-12-01
Keywords
Biochemistry
Department
Department of Biochemistry and Cell Biology
Language
en_US
Source
This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.
Identifier
http://hdl.handle.net/11401/76889
Publisher
The Graduate School, Stony Brook University: Stony Brook, NY.
Format
application/pdf
Abstract
The human de novo purine biosynthetic pathway consists of six proteins, which come together to form a protein complex called the purinosome. The tri-functional enzyme, TGART, which contains three domains, is one of the purinosome proteins. Protein-protein interaction studies have shown that TGART, along with two other de novo purine pathway proteins FGAMS and PPAT, is at the core of purinosome complex. Little is known, however about the interacting surface, stoichiometry or interaction mechanism. In order to understand this, we hope to solve the X-ray crystal structure of full-length human TGART, run quantitative protein interaction measurements on TGART, FGAMS and PPAT and decipher the molecular organization of these proteins. To date all three individual domains as well as a fusion domain with last two of the three domains of TGART have been expressed and purified to homogeneity. | 30 pages
Recommended Citation
Chitrakar, Iva, "Characterization of Trifunctional Glycinamide Ribonucleotide Synthetase and its Role in Purinosome Complex" (2014). Stony Brook Theses and Dissertations Collection, 2006-2020 (closed to submissions). 2763.
https://commons.library.stonybrook.edu/stony-brook-theses-and-dissertations-collection/2763