[Socbin] PhD and postdoc positions at Stockholm University

[Arne Elofsson]

Dear friends

I have two Phd and/or postdoc positions available.

Please forward this to any good candidates and ask them to contact me asap

yours

Arne


The research environment We sincerely believe that the research environment
at CBR is second to none when it comes membrane protein research. We provide
a unique environment combining theoretical studies with experimental work.
It is our goal that all students and postdocs in our lab should develop into
excellent scientists.

CBR <http://www.cbr.su.se/> is a strategic center for Biomembrane Research
at Stockholm University. CBR is funded by a strategic initiative to advance
Swedish research on membranes, membrane proteins, and cell membrane related
functionality. CBR hosts 19 internationally competitive research labs. One
area of expertise is theoretical studies of membrane proteins, where the
groups of von Heijne, Elofsson and Lindahl all have contributed
significantly. Today the Elofsson group consist of 9 PhD students (3
experimental and 6 computational) and 4 postdocs (1 experimental and 3
theoretical).
General information In general Postdoc positions are guaranteed for two
years, while the PhD positions are 4.5 year positions, including 6 month of
teaching. For all positions please contact me directly before applying. For
all positions we can offer competitive pay.

 PhD/postdoc position within "Studies of membrane protein structure, folding
and evolution." Membrane proteins are the gateways to the cells and as such
they are of great importance for the development of drugs. The translation
of integral alpha-helical membrane proteins by the ribosome is halted when
the signal peptide is recognized by a signal recognition particle. Then, the
ribosome is transported to the ER where translation continues with the
emerging peptide chain threaded through the translocon channel.
Traditionally, these TM-proteins have been thought to consist of long
hydrophobic alpha-helices that span the membrane connected through loops,
which are folded by a two-step process. However, recent studies in our lab
and elsewhere have shown that the structural repertoires of membrane
proteins is much more complex than was believed only a few years and the
simple two-state model cannot fully explain their folding.

The primary aim of this project is to use computational method to understand
the structure, folding and evolution of membrane proteins. Primarily, the
project is focused on the development of a method to perform simulations of
the insertion mechanism of alpha-helices into the membrane. These
simulations will then be performed in close collaboration with our
experimental work.

A general interest in protein, biophysics and programming and a solid
background in bioinformatics, physics or computer science is suitable for
this position.
PhD/Postdoc position in "Human proteome evolution and variation." Evolution
of individual genes has been studied for decades, however most of the focus
has been on two mechanism, the mutations, insertions or deletion of a few
nucleotides/amino-acids and the duplication of complete genes (or
chromosomes/genomes). However, these two mechanisms do not provide a
complete picture of protein evolution, in particular if seen over a longer
perspective. In particular recent studies of human genetic variation has
highlighted that "mutations" that includes insertions, deletion or
duplication of longer regions than singly nucleotides.

We have, in a set of recent papers, significantly increased our
understanding of the mechanisms and behind, and constraints for, protein
domain evolution and the interaction between protein domains. Most
importantly, we have shown that domain fusion mainly occurs through a simple
mechanism of fusing one domain at a time at the N- or C-terminal. This
simplistic picture is surprisingly robust. However, there is one notable
exception to this rule, proteins consisting of repeating domains. We have
discovered that the repeated domains are instead frequently added several at
a time and not necessarily at the N or C-terminus

Within this project the goal is to extend our earlier studies with all the
genomic data that rapidly is being generated. A general interest in protein
evolution and a solid background in bioinformatics, biotechnology, physics
or chemistry is suitable for this position.
More information

   - http://bioinfo.se/papers/
   - http://www.cbr.su.se/
   - Mail me for more info



Yours

Arne

---------------------------------------------------------
Prof.  Arne Elofsson      Dep of Biochemistry and Biophysics
Tel:+46-8-16 4672      Stockholm University
Fax:+46-8-15 3679      10691 Stockholm, Sweden
Directions: see http://bioinfo.se/misc/directions.html
Net: arne at bioinfo.se   http://bioinfo.se/
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