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Investigating the function of GroES with hard-to-fold proteins in vivo
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Clinical and Experimental Medicine. Linköping University, Faculty of Medicine and Health Sciences.
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2019 (English)Student paper other, 10 credits / 15 HE creditsStudent thesis
Abstract [en]

The use of molecular chaperones can increase the yield of correctly folded proteins. This is especially needed in the expression of proteins non-native to the host organism. This study set out to investigate the function of the chaperone GroES; a component in the GroE-system. The function of this chaperone has only been studied alone in vitro. Here we lay ground to further studies on GroES and its ability to act alone in vivo. GroES was expressed from a plasmid and characterized through its potential to increase the amount of correctly folded proteins. Characterization was mainly done by fluorescence spectroscopy with hard-to-fold proteins linked to fluorescent probes. Results show a very clear increase in fluorescence for most of the substrate proteins tested, indicating that GroES has a significant role in the GroE-system and perhaps outside of it.

Place, publisher, year, edition, pages
2019. , p. 29
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-154170OAI: oai:DiVA.org:liu-154170DiVA, id: diva2:1284145
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Available from: 2019-02-11 Created: 2019-01-31 Last updated: 2019-02-11Bibliographically approved

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ChemistryFaculty of Science & EngineeringDepartment of Clinical and Experimental MedicineFaculty of Medicine and Health Sciences
Biochemistry and Molecular Biology

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CiteExportLink to record
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Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
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  • asciidoc
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