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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 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.