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 [log in to unmask] or
[log in to unmask] 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.
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