Thesis
Protein microenvironments for topology analysis
- Creator
- Rights statement
- Awarding institution
- University of Strathclyde
- Date of award
- 2016
- Thesis identifier
- T14464
- Person Identifier (Local)
- 200956226
- Qualification Level
- Qualification Name
- Department, School or Faculty
- Abstract
- Amino Acid Residues are often the focus of research on protein structures. However, in a folded protein, each residue finds itself in an environment that is definedby the properties of its surrounding residues. The term microenvironment is usedherein to refer to these local ensembles. Not only do they have chemical properties but also topological properties which quantify concepts such as density,boundaries between domains and junction complexity. These quantifications areused to project a protein’s backbone structure into a series of scores.The hypothesis was that these sequences of scores can be used to discover proteindomains and motifs and that they can be used to align and compare groups of3D protein structures.This research sought to implement a system that could efficiently compute microenvironments such that they can be applied routinely to large datasets. Thecomputation of the microenvironments was the most challenging aspect in termsof performance, and the optimisations required are described.Methods of scoring microenvironments were developed to enable the extractionof domain and motif data without 3D alignment. The problem of allosteric sitedetection was addressed with a classifier that gave high rates of allosteric sitedetection.Overall, this work describes the development of a system that scales well withincreasing dataset sizes. It builds on existing techniques, in order to automatically detect the boundaries of domains and demonstrates the ability to processlarge datasets by application to allosteric site detection, a problem that has notpreviously been adequately solved.
- Advisor / supervisor
- Wilson, John
- Dufton, Mark
- Resource Type
- Note
- Previously held under moratorium from 1st December 2016 until 1st December 2021
- DOI
- Date Created
- 2016
- Former identifier
- 9912537892902996
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PDF of thesis T14464 | 2021-07-02 | Público | Baixar |