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Affiliations

• Bioscience

Education Profile

• ​​​​​​​​​​PhD, University of Warsaw, Poland, 2012
• MSc, University of Wroclaw, Poland, 2008

Research Interests

​The research of Professor Łukasz Jaremko is focused on atomic-level insight into essential and topical questions of biochemistry and molecular medicine.

Biomolecular nuclear magnetic resonance (NMR) spectroscopy is the key experimental technique used and developed in the lab to tackle challenging macromolecular assemblies. The NMR-based structural studies are often combined with molecular biology and other state-of-the-art biophysical techniques: X-ray crystallography, circular dichroism and molecular dynamics simulations.

The cutting-edge biological NMR spectroscopy gives access to both structure and dynamics, thus providing information on functioning of essential macromolecular systems and their mutual interactions under close-to-native conditions (like aqueous solutions at physiological temperature, lipid membranes, living cell environment). The mutual complementarity between NMR and remaining powerful high-resolution experimental techniques (X-ray crystallography and cryo-electron microscopy) paves the way to more complete description of the pivotal biochemical processes of life and disease.

Selected Publications

• Gray, F., Cho, H.-J., Shukla. S., He S., Harris A., Boytsov B., Jaremko L., Jaremko M., Demeler, B., R. Lawlor, R. E., Grembecka, J., Cierpicki, T. (2016) BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization, Nature Communications, 7:13343.;
  
• Jaremko, M., Jaremko, L., Villinger, S., Schmidt, C., Giller, K., Griesinger C., Becker, S., Zweckstetter, M. (2016) High resolution determination of the dynamic structure of membrane proteins, Angewandte Chemie International Edition, 55, 10518-10521;
  
• Jaremko, L., Jaremko, M., Nowakowski, M., Ejchart, A. (2015) The quest for simplicity - remarks on the free-approach models, Journal of Physical Chemistry B, 119, 11978-11987;
  
• Jaremko, L., Jaremko, M., Giller, K., Becker, S., Zweckstetter, M. (2014) Structure of the mitochondrial translocator protein in complex with a diagnostic ligand, Science, 343, 1363-1366;
  
• ​Jaremko, L., Jaremko, M., Elfaki, I., Mueller, J. W., Ejchart, A., Bayer, P., Zhukov, I. (2011) Structure and dynamics of the first archaeal parvulin reveal a new functionally important loop in parvulin-type prolyl isomerases., Journal of Biological Chemistry, 286, 6554-6565.