{"@context":"http://iiif.io/api/presentation/2/context.json","@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/manifest.json","@type":"sc:Manifest","label":"Characterization of Trifunctional Glycinamide Ribonucleotide Synthetase and its Role in Purinosome Complex","metadata":[{"label":"dc.description.sponsorship","value":"This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree."},{"label":"dc.format","value":"Monograph"},{"label":"dc.format.medium","value":"Electronic Resource"},{"label":"dc.identifier.uri","value":"http://hdl.handle.net/11401/76889"},{"label":"dc.language.iso","value":"en_US"},{"label":"dc.publisher","value":"The Graduate School, Stony Brook University: Stony Brook, NY."},{"label":"dcterms.abstract","value":"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."},{"label":"dcterms.available","value":"2017-09-20T16:51:23Z"},{"label":"dcterms.contributor","value":"French, Jarrod B"},{"label":"dcterms.creator","value":"Chitrakar, Iva"},{"label":"dcterms.dateAccepted","value":"2017-09-20T16:51:23Z"},{"label":"dcterms.dateSubmitted","value":"2017-09-20T16:51:23Z"},{"label":"dcterms.description","value":"Department of Biochemistry and Cell Biology"},{"label":"dcterms.extent","value":"30 pg."},{"label":"dcterms.format","value":"Monograph"},{"label":"dcterms.identifier","value":"http://hdl.handle.net/11401/76889"},{"label":"dcterms.issued","value":"2014-12-01"},{"label":"dcterms.language","value":"en_US"},{"label":"dcterms.provenance","value":"Made available in DSpace on 2017-09-20T16:51:23Z (GMT). No. of bitstreams: 1\nChitrakar_grad.sunysb_0771M_12148.pdf: 2259603 bytes, checksum: 6b96a066b6470533246f244fd1bd0f19 (MD5)\n  Previous issue date:    1"},{"label":"dcterms.publisher","value":"The Graduate School, Stony Brook University: Stony Brook, NY."},{"label":"dcterms.subject","value":"Biochemistry"},{"label":"dcterms.title","value":"Characterization of Trifunctional Glycinamide Ribonucleotide Synthetase and its Role in Purinosome Complex"},{"label":"dcterms.type","value":"Thesis"},{"label":"dc.type","value":"Thesis"}],"description":"This manifest was generated dynamically","viewingDirection":"left-to-right","sequences":[{"@type":"sc:Sequence","canvases":[{"@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/canvas/page-1.json","@type":"sc:Canvas","label":"Page 1","height":1650,"width":1275,"images":[{"@type":"oa:Annotation","motivation":"sc:painting","resource":{"@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/40%2F23%2F91%2F40239130916328591508593001688984997216/full/full/0/default.jpg","@type":"dctypes:Image","format":"image/jpeg","height":1650,"width":1275,"service":{"@context":"http://iiif.io/api/image/2/context.json","@id":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/40%2F23%2F91%2F40239130916328591508593001688984997216","profile":"http://iiif.io/api/image/2/level2.json"}},"on":"https://repo.library.stonybrook.edu/cantaloupe/iiif/2/canvas/page-1.json"}]}]}]}