The study of proteins and their function is key to understanding the intrinsic properties of the cell both in normal and disease states. An important part of this analysis involves the prediction and elucidation of three-dimensional protein structures, and the interactions they undertake, through the use of computational techniques. The majority of work in this thesis focuses on the effects that non-specific charge interactions have on these structures. Firstly, sets of proteins that select a single partner from closely related alternatives were analysed using an empirical binding model in order to identify a determinant for binding specificity. Here, we predicted that charge interactions are more favourable in the majority of cognate pairs, compared to other energetic and geometric properties. In addition to this, charged protein side-chains were found to be important with respect to phosphorylation sites that lie in disordered regions of proteins. The analysis of charge environments around these sites indicated a propensity for a subset of residues to be phosphorylated when surrounded by charged residues. This was especially true for proteins involved in RNA processing.An investigation of protein-mRNA interactions also identified a role for charge interactions that occur within translational control mechanisms. The correlation seen between positively charged disordered regions of specific regulatory proteins and the secondary structure of target mRNAs revealed a potential control mechanism that is partially influenced by polyelectrostatic interactions.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:564357 |
| Date | January 2012 |
| Creators | Cawley, Andrew |
| Contributors | Warwicker, Jim |
| Publisher | University of Manchester |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | https://www.research.manchester.ac.uk/portal/en/theses/a-computational-study-of-polyelectrostatic-interactions-in-proteins(f7b52529-4dfd-4c4b-92b9-112b0ba5ef44).html |
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