Medicine and Biotechnology at Heinrich-Heine-University Düsseldorf in
Germany, funded by the Ministry of Innovation, Science, Research and
Technology of the German Federal State North Rhine-Westphalia (NRW),
and the school chairmen Prof. Dr. Lutz Schmitt and Prof. Dr. Dieter
Willbold invite applications for a PhD Scholarship starting in October 2011.
BioStruct offers innovative PhD education and research programs within
a stimulating interdisciplinary environment combining the field of
structural biology with molecular medicine and biotechnology.
Highly motivated and excellent candidates holding an MSc or Diploma
degree in the fields of Biochemistry, Biology, Chemistry, Physics and
related fields can directly apply for a scholarship including a
monthly stipend of 1345,- EUR and contributions towards travel and
research expenses.
1. PhD Scholarship for ‘Structural studies on molecular interactions
of the Disrupted-in-schizphrenia (DISC1) protein'
The ideal candidate will have a background in protein biochemistry
and/or biophysical characterization of proteins. Basic knowledge
and/or experience in crystallization and X-ray spectroscopy would be
an advantage. A strong interest in structural biology is a
prerequisite. We are looking for an enthusiastic and highly motivated
individual with fluency in written and spoken English, an open mind
for new approaches and a lot of team spirit.
Workplace will be the “University hospital Düsseldorf” at
Prof. Dr. Korth's Lab
/Research Group Neurodegeneration Neuropathology.
PhD Research Project Summary: The molecular causes of schizophrenia
are still unknown. Recently, based on several genetic studies, the
disrupted-in-schizophrenia 1 (DISC1) protein has come into focus for
investigating molecular mechanisms of schizophrenia and other mental
diseases. Here, structural and quantitative investigations of DISC1
with its interacting centrosomal molecules NDEL1, NDE1, PDE4B and LIS1
are proposed. All proteins, or soluble representative fragments
thereof, as well as mutant / polymorphic counterparts will be
expressed in Escherichia coli. Structural studies will be attempted by
NMR and crystallography for single and complexed proteins and
complemented by binding studies with surface plasmon resonance.
These investigations will yield insight into the stochiometry and
regulation of the interactions in the DISC1/NDEL1/NDE1/LIS1/PDE4B
complex, and, through structural determination of binding interfaces,
open novel pharmacological targets for these diseases.
2. PhD Scholarship for ‘Protein Structure Determination of
Proton-translocating pyrophosphatases using X-ray crystallography’
The ideal candidate will have a background in membrane protein
expression and purification as well as in biophysical characterization
of proteins. Basic knowledge and/or experience in protein
crystallisation would be an advantage. A strong interest in structural
biology is a prerequisite.
Workplace will be the “Heinrich Heine University Düsseldorf” in the
group of Prof. Dr. Georg Groth.
PhD Research Project Summary: Transmembrane proton pumping is
responsible for many physiological processes including the generation
of proton motive force that drives bioenergetics. Among the various
proton pumping enzymes, vacuolar pyrophosphatases (V-PPases) form a
distinct class of proton pumps, which are characterised by their
ability to translocate protons across a membrane by using inorganic
pyrophosphate (PPi) instead of ATP as an energy source.
The project will be directed at gaining a fundamental understanding of
the structure and molecular mechanism of inorganic pyrophosphate-
(PPi-) energized proton pumps using x-ray crystallography.
3. PhD Scholarship for ‘Structure and function of the Chlamydia
adhesins OmcB and Pmp21'
The ideal candidate will have a background in protein biochemistry and
biophysical characterization of proteins. A strong interest in
infection biology as well as in structural biology is a prerequisite.
Workplace will be the “Heinrich Heine University Düsseldorf” in the group of Prof. Dr. Johannes Hegemann.
PhD Research Project Summary: Chlamydiae are obligate intracellular
bacterial pathogens which cause a variety of important human diseases.
Chlamydia trachomatis is the most common bacterial agent of sexually
transmitted diseases and is responsible for over 90 million new
infections every year worldwide. The C. trachomatis ocular serovars
are responsible for trachoma, the major cause of preventable blindness
in developing countries. Acute C. pneumoniae infections cause
pulmonary diseases (e.g. 10 % of all pneumonia incidents worldwide),
whereas the chronic infection is linked to atherosclerosis and artery
disease. The chlamydial infection starts with the adhesion of the
bacteria to the human cell by binding of bacterial adhesins to
eukaryotic receptors.
We have identified and characterised the first chlamydial adhesin
proteins which interact with the human cell. The OmcB protein binds to
heparan sulfate-like glycosaminoglycan (GAG) structures on the human
cell surface. Single amino acids in the GAG-binding domain of OmcB are
essential for adhesion to human cells and may determine cell tropism
and disease pattern for different C. trachomatis serovars (systemic
versus local infection). The second adhesin recently identified
consists of a family of 21 related polymorphic membrane proteins (Pmp)
unique to Chlamydiae, whose human cell surface receptor has just been
identified. Pmp proteins are anchored in the bacterial membrane and
their N-termini carry several independent adhesion domains.
Analysis of the three-dimensional structure of the adhesins OmcB and
Pmp21 (as prototype) will form the basis for a molecular understanding
of the interactions of these proteins with their human receptors and
will facilitate identification of small molecule inhibitors.
4. PhD Scholarship for the project "Conformational dynamics and
structure of biomolecules studied by super-resolution Förster
Resonance-Energy-Transfer (FRET)"
The ideal candidate will have a background in biophysical principles
of biomolecular function (RNA and proteins). A strong interest in
structural biology and fluorescence spectroscopy is a prerequisite.
Workplace will be the “Heinrich-Heine-University” in the group of
Prof. Dr. Claus Seidel.
PhD Research Project Summary: While X-ray crystallography reveals
snapshots of biomolecules at atomic resolution, many biomolecules are
inherently dynamic. In some cases, low populated conformational states
are overlooked or simply not accessible using conventional structural
biology tools.
FRET that is considered a low-resolution tool has not yet received
much attention in the field. However, recent developments in Prof.
Seidel's group have shown the ability to reconstruct nucleic acid
structures using super-resolution FRET [Methods in Enzymology 475,
455-514 (2010), J. Am. Chem. Soc. 133, 2463-2480 (2011)].
We propose to use these recent tools ensemble and single-molecule
spectroscopy to determine super-resolution FRET structures of multiple
conformational states in biomolecules. A special focus is on detailed
characterization and 3D architecture of helical structures. Using all
fluorescence techniques the 3D structures of complex, temperature
sensitive regulatory RNA "thermometers" with a varying number of stem
loops shall be solved in this project. Moreover we will use these
tools to study helix bending und rotation of transmembrane helices in
membrane proteins studied in our group.
For further information on the NRW Research School BioStruct,
prerequisites and mandatory application forms
please visit our website:
Application Deadline: August 26th, 2011 Only complete applications according to the BioStruct application regulations will be considered. For further information please visit: www.biostruct.de
Application details: http://www.uni-duesseldorf.de/home/Fakultaeten/math_nat/Graduiertenkollegs/biostruct/Application/Scholarship