Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/2469
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dc.coverage.spatialen_US
dc.date.accessioned2011-08-26T12:17:31Z-
dc.date.available2011-08-26T12:17:31Z-
dc.date.issued2011-08-26-
dc.identifier.urihttp://hdl.handle.net/10603/2469-
dc.description.abstractThe main aim of structural biology has been to understand how a protein functions based on its structure. This approach has been remarkably successful but with a side-effect that proteins or regions in proteins which do not have a well defined three dimensional structure (also called as disordered regions/proteins) have been ignored. The limitations of experimental methods in studying these regions have also not helped. But these proteins/regions can no longer be ignored not only because they are exciting to study but also because they are surprisingly common in eukaryotes. Computational methods to predict disordered regions in proteins have advanced rapidly. Concurrently, genome wide functional data, particularly for yeast has become available. I took advantage of these resources to find associations between predicted disorder and various functional data to increase our understanding of the functional roles of disordered regions/proteins. newline I find significant association between protein disorder and PEST regions in proteins, which are involved in rapid degradation of proteins, suggesting that PEST regions mediate rapid degradation of proteins due to their disorderedness. I also find that hubs in the protein interaction networks, which interact with their partners in transient manner, tend to be more disordered. This finding in protein-protein interaction networks is extended to transcriptional regulatory networks, wherein I find that transcription factor hubs tend to be more disordered than non-hub transcription factors. Further, I find that expression levels and aggregation propensity of proteins also influence their disorderness. newline Overall these results suggest that structural disorder in proteins does not mean functional disorderness, but that disorder regions/proteins are crucial in the functioning of biological systems, particularly eukaryotic organisms.en_US
dc.format.extent94p.en_US
dc.languageEnglishen_US
dc.relationen_US
dc.rightsuniversityen_US
dc.titleUnderstanding the functional significance of intrinsically disordered regions in proteins using computational methodsen_US
dc.title.alternativeen_US
dc.creator.researcherSingh, Gajinder Palen_US
dc.subject.keywordBiotechnologyen_US
dc.description.noteAbstract includes, References p.66-81, Supplementary information p.82-94en_US
dc.contributor.guideDash, Debasisen_US
dc.publisher.placePuneen_US
dc.publisher.universityUniversity of Puneen_US
dc.publisher.institutionInstitute of Genomics and Integrative Biologyen_US
dc.date.registered0en_US
dc.date.completedJune, 2009en_US
dc.date.awarded2009en_US
dc.format.dimensionsen_US
dc.format.accompanyingmaterialDVDen_US
dc.type.degreePh.D.en_US
dc.source.inflibnetINFLIBNETen_US
Appears in Departments:Institute of Genomics and Integrative Biology

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01_title.pdfAttached File62.01 kBAdobe PDFView/Open
02_certificate.pdf33.6 kBAdobe PDFView/Open
03_declaration.pdf19.52 kBAdobe PDFView/Open
04_acknowledgements.pdf20.91 kBAdobe PDFView/Open
05_table of contents.pdf51.03 kBAdobe PDFView/Open
06_list of figures and tables.pdf61.56 kBAdobe PDFView/Open
07_abbreviations.pdf18.15 kBAdobe PDFView/Open
08_abstract.pdf19.86 kBAdobe PDFView/Open
09_chapter 1.pdf181.87 kBAdobe PDFView/Open
10_chapter 2.pdf213.87 kBAdobe PDFView/Open
11_chapter 3.pdf250.6 kBAdobe PDFView/Open
12_chapter 4.pdf274.07 kBAdobe PDFView/Open
13_chapter 5.pdf291.18 kBAdobe PDFView/Open
14_references.pdf119.4 kBAdobe PDFView/Open
15_supplementary information.pdf1.01 MBAdobe PDFView/Open


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