Postdoctoral position protein engineering and biocatalysis (1.0 fte)
In order to pursue our research activities, we are looking for a highly motivated postdoc who will contribute to an NWO-ECHO project in the field of protein engineering and biocatalysis. This project aims to exploit the promiscuous Michael-type addition activity of 4-oxalocrotonate tautomerase as a starting point to develop novel synthetically useful C-C bond-forming enzymes, as well as to provide insight into the manner in which a promiscuous protein might evolve to acquire more active and specific enzyme functions (see: Van der Meer et al., 2016, Nat. Commun. 7:10911 doi: 10.1038/ncomms10911). The key objectives are to 1) use a highly informative systematic mutagenesis approach to rapidly scan the whole 4-OT protein to create a map of neutral, beneficial and detrimental amino acids for each position and for each of its promiscuous C-C bond-forming ‘Michaelase' activities, 2) test if identified ‘hotspot' positions in 4-OT can drive the molecular evolution of more specific and active ‘Michaelase' functions, and determine which of the changes to these positions have additive, synergistic, or antagonistic effects, and 3) characterize the biocatalytic and structural properties of the newly evolved ‘Michaelases'. The postdoc will be involved in the supervision of PhD students, who are working on protein engineering and biocatalysis, and are funded by other NWO and EU projects.
This job comes from a partnership with Science Magazine and