A two year postdoctoral position in protein NMR is open at the department of chemistry, University of Umeå, Sweden. The research in our group is focused on understanding the cooperativity of conformational change and protein folding. To this end we have established suitable model systems. The direction of research for the open position will depend on the interests of the candidate.
We are using state of the art NMR experiments, such as relaxation dispersion, to quantify conformational exchange dynamics. In addition we use ultrafast SOFAST-HMQC experiments to measure hydrogen exchange which is an extremely useful tool in many cases. Protein engineering is an integral part of all our research projects. Structure determination is pursued when necessary.
The department harbors two high field Bruker NMR spectrometers, one 500 MHz instrument equipped with a warm probe and one 600 MHz instrument equipped with a cold triple resonance probe. In addition, we have access to both 800 and 900 Varian spectrometers located at the Swedish NMR centre in Gothenburg; these instruments can be operated remotely from our lab.
We are seeking candidates with documented skills in solution state protein NMR, including quantification of dynamics and /or structure determination. The candidate must have a Ph. D.
Contact information:
Dr. Magnus Wolf-Watz
Department of Chemistry
University of Umeå
Sweden
Email:
magnus.wolf-watz@chem.umu.se
Phone: +46-90-786 76 90
Lab website:
www.chemistry.umu.se
References:
1. Åden J., & Wolf-Watz M. (2007), JACS, 14, 14003-14012.
2. Wolf-Watz M., et al. (2004), Nat. Struct. Mol. Biol. ,11, 945-949.
3. Henzler-Wildman K., et al. (2007), Nature, 2007, 450, 838.