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Investigation of the interactions between the bacterial homologue to actin, and the chaperone GroEL/ES through a combination of protein engineering and spectroscopy
Linköping University, Department of Physics, Chemistry and Biology.
2008 (English)Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesisAlternative title
Undersökning av interaktionerna mellan MreB, den bakteriella homologen till aktin, och chaperonet GroEL/ES genom en kombination av protein engineering och spektroskopi (Swedish)
Abstract [en]

Molecular chaperones help many proteins in the cell reach their native conformation. The mechanism with which they do this has been studied extensively, but has not been entirely elucidated. This work is a continuation of the study done by Laila Villebeck et al. (2007) on the conformational rearrangements in the eukaryotic protein actin in interaction with the eukaryotic chaperone TRiC. In this study the intentions were to analyze the protein MreB, a prokaryotic homologue to actin, when interacting with the prokaryotic chaperone GroEL. The purpose was to investigate if the mechanisms of GroEL and TRiC are similar. The analysis of the conformation of MreB was to be made through calculations of fluorescence resonance energy transfer (FRET) between two positions in MreB labeled with fluorescein. A MreB mutant was made through site-specific mutagenesis to enable labeling at a specific position. Another single mutant and a corresponding double mutant needed for these measurements were avaliable from earlier studies. The results from fluorescence measurements on these mutants indicated that the degree of labeling was insufficient for accurate determination of FRET. Suggestions are made on improvements of the experimental approach for future studies.

Place, publisher, year, edition, pages
2008. , 45 p.
Keyword [en]
Site-directed mutagenesis, protein engineering, fluorescence, FRET, chaperone
Keyword [sv]
Site-specifik mutagenes, protein engineering, fluorescens, FRET, chaperon
National Category
Natural Sciences
URN: urn:nbn:se:liu:diva-15818ISRN: LITH-IFM-A-EX--08/2030—SEOAI: diva2:160414
Subject / course
Chemical Biology
Physics, Chemistry, Mathematics
Available from: 2009-02-18 Created: 2008-12-07 Last updated: 2011-10-26Bibliographically approved

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Blom, Lillemor
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