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Structural and functional studies of Sirtuin-Substrate-protein complexes

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Institution information: The group links the SFB635 (Post-translational control of protein function) and the CECAD (The Cologne Cluster of Excellence in Cellular Stress Responses in Aging-associated Diseases).

Website: http://cecad.uni-koeln.de/Dr-Michael-Lammers.94.0.html

Location: The group is located at the CECAD Research Center, University of Cologne Joseph-Stelzmann-Str. 26, 50931 Cologne, Germany. The Cologne research community including the University of Cologne, the University Hospital of Cologne, the CECAD and the Max-Planck-Institute for Biology of Aging is a highly stimulating and international academic research environment.

Summary: Regulation of protein function by lysine-acetylation has only been marginally investigated so far. Recent progress in quantitative mass spectrometry has demonstrated that thousands of non-histone proteins are acetylated in mammalian cells in all cellular compartments. To target lysine-deacetylases has a huge therapeutic potential and indeed several drugs inhibiting certain lysine-deacetylases are in clinical trials or even on the market to treat neurodegenerative diseases and cancer. A major drawback however is, that those compounds often have substantial unwanted off-target effects due to a lack of specificity. We want to use the genetic-code expansion concept to incorporate acetyl-lysine into deacetylase substrate proteins to characterize these interactions functionally and structurally. Indeed, structural data of a deacetylase in complex with a natively-folded substrate protein is not available and is one of the major aims of this thesis. This would be an important step further to develop more specific compounds targeting the lysine-deacetylase machinery. Deregulation and aberrations in deacetylase expression levels or activities has been shown to contribute  to the development of severe cellular diseases resulting in neurodegenerative disorders and cancer. A strategy to produce therapeutic deacetylase inhibitors is the use of mechanistic inhibitors such as trifluoroacetyl-lysine. We want to optimize a system to site-specifically incorporate trifluoroacetyl-lysine into natively-folded proteins using the genetic-code expansion concept in E. coli or yeast.

Job description: We search for a highly motivated student with profound knowledge in proteinbiochemistry (protein-purification, -expression in E. coli). We will perform various biophysical assays (isothermal-titration calorimetry, fluorescence assays, stopped-flow, X-ray crystallography, etc.).

Qualification: Applicants must have a Bachelor of Science degree in biology /biochemistry/biophysics or related subject. Solid experience in proteinbiochemistry (including protein-purification/-expression), is advantagous but not a must. Additionally, knowledge in cell biology is advantagous. Profound experience in molecular biological methods (cloning, mutagenesis, western blotting, etc.) is essential.

How to Apply: Send a short cover letter, CV, certificates and address of one scientific reference as single PDF-document to michael.lammers@uni-koeln.de.

Contact detail

How to apply:
How to Apply: Send a short cover letter, CV, certificates and address of one scientific reference as single PDF-document to michael.lammers@uni-koeln.de
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Job profile

Working hours
Contract duration
Type of job
Diploma Thesis/Master's Thesis
Work experience
job experience is not required
Germany (Nordrhein-Westfalen)
Working place
50931 Cologne, Germany
Area of expertise
Biology & Life Sciences