The
non-ribosomal peptide synthetases (NRPSs) constitute a large group of
biosynthetic enzymes found in both bacteria and fungi responsible for
producing a wide range of bioactive polypeptides. Well-known examples of
products synthesized by NRPSs are the antibiotic penicillin and the
immunosuppressant cyclosporin, used during kidney transplant surgery to
prevent organ rejection. However, the vast majority of fungal NRPSs are
currently unexplored and this group of enzymes therefore holds a huge
potential for development of novel pharmaceuticals.
Within the AUFF Centre for Natural Non-Ribosomal Peptide Synthesis (NANORIPES), Department of Molecular Biology and Genetics, Aarhus University a 2 year post doc position is available starting 1 March 2013. The aim of the post doc project is investigation of the structure and function of NRPS enzymes present in species of the crop pathogen, Fusarium to eventually be able to predict the biomedical potential of unknown NRPSs. The project involves structural and functional studies of individual synthetase specificity domains and their complexes with the compounds they bind. The experimental approach involves protein expression and purification as well as structure determination by x-ray crystallography. Structures of ligand-bound enzyme domains will then subsequently be studied in collaboration with chemists identifying the bound amino acids.
For more information please contact Associate Professor Ditlev Brodersen, deb@mb.au.dk, +45 21669001.
Within the AUFF Centre for Natural Non-Ribosomal Peptide Synthesis (NANORIPES), Department of Molecular Biology and Genetics, Aarhus University a 2 year post doc position is available starting 1 March 2013. The aim of the post doc project is investigation of the structure and function of NRPS enzymes present in species of the crop pathogen, Fusarium to eventually be able to predict the biomedical potential of unknown NRPSs. The project involves structural and functional studies of individual synthetase specificity domains and their complexes with the compounds they bind. The experimental approach involves protein expression and purification as well as structure determination by x-ray crystallography. Structures of ligand-bound enzyme domains will then subsequently be studied in collaboration with chemists identifying the bound amino acids.
For more information please contact Associate Professor Ditlev Brodersen, deb@mb.au.dk, +45 21669001.
Application Deadline : 10 February 2013
