Max Planck Institute for Developmental Biology
Tuebingen, Germany.
PhD or postdoctoral positions funded by tax free fellowships are available in the research group of Remco Sprangers and in the research group of Silke Wiesner. We are looking for candidates that have a strong interest structural biology and biochemistry. More details about the projects that combine NMR spectroscopy, X-ray crystallography and biochemical approaches can be found below. Both laboratories are very well equipped, including new 600 and 800 MHz NMR spectrometers, crystallization robots and state-of-the-art instrumentation for protein expression and purification. In addition, we have regular access to the synchrotron facility at the SLS.
Applicants for the PhD positions should have a strong background in biochemistry, chemistry and/or biophysics. Applicants for the postdoctoral positions should have a PhD in NMR spectroscopy or X-ray crystallography. Please contact remco.sprangers@tuebingen.mpg.de or silke.wiesner@tuebingen.mpg.de by June 15, 2011 and include a pdf file with a brief CV, names of two referees and a summary of research interests and previous research projects.
The research group of Remco Sprangers (http://www.eb.tuebingen.mpg.de/research-groups/remco-sprangers) studies how protein motions determine enzymatic function. We are especially interested in the machinery that degrades mRNA. Structural changes in the degradation complex allow for a tight regulation of the mRNA decay process that is crucial for cellular homeostasis. To understand how this is achieved on an atomic level, we use novel techniques in high resolution NMR spectroscopy (methyl TROSY) in combination with X-ray crystallography and biochemical experiments.
The research group of Silke Wiesner (http://www.eb.tuebingen.mpg.de/research-groups/silke-wiesner) is interested in the structure, function, and regulation of the ubiquitination machinery. Ubiquitination marks proteins for degradation and thereby controls cellular signaling and behavior. We seek to provide a molecular basis for protein ubiquitination and to understand how diseases like cancer arise from dysfunctional ubiquitination enzymes. We gain structural information from NMR and/or X-ray crystallography and combine this information with investigations targeted at functional aspects using both in vitro and in vivo studies.
