Posttranslational modifications (PTMs) of proteins represent fascinating extensions of the dynamic complexity of living cells' proteomes, but also present a solid obstacle in the proteome analysis. Identification and mapping of PTMs in proteins have improved dramatically, but to comprehend complex mechanisms and biological functions, one must address also a very low abundant proteins. Here, in this thesis entitled 'Analysis of DELLA protein ubiquitination' we demonstrate the use of a recombinant protein standard for the determination of in vivo modified peptides of the DELLA family protein RGA. The candidate peptide sequences were targeted in an SRM-based analysis to detect the ubiquitination site and the results of this analysis and that of an MS/MS data processing indicate that the modification is localized in the conserved N-terminal region of RGA protein.
| Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:362659 |
| Date | January 2016 |
| Creators | Breineková, Alžběta |
| Source Sets | Czech ETDs |
| Language | Czech |
| Detected Language | English |
| Type | info:eu-repo/semantics/masterThesis |
| Rights | info:eu-repo/semantics/restrictedAccess |
Page generated in 0.0902 seconds