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Strukturella och funktionella studier av fyra enzymer involverade i cellväggsbiosyntes hos Mycobacterium tuberculosis
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Biology Education Centre.
2015 (Swedish)Independent thesis Advanced level (professional degree), 20 credits / 30 HE creditsStudent thesisAlternative title
Structural and functional studies of four enzymes involved in Mycobacterium tuberculosis cell wall biosynthesis (English)
Abstract [en]

The pathogenic bacterium Mycobacterium tuberculosis (Mt) is the causative agent of tuberculosis, a widespread and fatal infectious disease. Today, treatment against tuberculosis involves a combination of drugs, which need to be taken for at least six months and which often causes severe side effects. Therefore, new drugs that are more effective and that give fewer side effects are needed. A characteristic feature of the Mt bacterium is its very complex and thick cell wall, which prevents many potential drug molecules from penetrating it. Inhibiting any one of the enzymes that are involved in its biosynthesis would therefore seem to be a good strategy for eliminating the Mt bacteria. The aim of this study was to characterize four enzymes involved in Mt cell wall biosynthesis. In order to do that, they were produced recombinantly in E. coli and purified. Crystallization experiments were set up in order to produce diffracting crystals, with the aim of structure determination and drug design.

Place, publisher, year, edition, pages
2015. , 62 p.
Series
UPTEC X, ISSN 1401-2138 ; 15 028
Keyword [en]
Mycobacterium tuberculosis, structure-based drug design, enzymes, cloning, expression, purification, crystallization
National Category
Pharmaceutical Biotechnology
Identifiers
URN: urn:nbn:se:uu:diva-264352OAI: oai:DiVA.org:uu-264352DiVA: diva2:860211
Educational program
Molecular Biotechnology Engineering Programme
Supervisors
Examiners
Available from: 2015-10-12 Created: 2015-10-09 Last updated: 2015-10-12Bibliographically approved

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CiteExportLink to record
Permanent link

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Citation style
  • apa
  • ieee
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  • de-DE
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  • en-US
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Output format
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