PhD, Institute of Biochemistry and Biophysics of Polish Academy of Sciences (IBB PAS), Warsaw, Poland, 2012
MSc, University of Wroclaw, Wroclaw, Poland, 2008
The research group of Professor Mariusz Jaremko is focused on understanding and describing the basic principles of protein folding and misfolding, as well as the behavior of peptides and Intrinsically Disordered Proteins (IDPs) under different conditions, including conditions as close as possible to the physiological ones. To achieve these scientific goals, the state-of-the-art techniques of biomolecular NMR spectroscopy, together with other biophysical tools, are used. Understanding the biological phenomena which rule the protein folding and dynamics would allow for the design of new safe and biodegradable materials with desired physico-chemical properties, as well as the rational design of new drugs and efficient therapies against numerous neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases, and other protein aggregation-related diseases, like diabetes type II.
Kadavath, H., Jaremko, M., Jaremko, L., Biernat, J., Mandelkow, E., Zweckstetter, M. (2015) Folding of Tau protein on microtubules, Angew. Chem. Int. Ed. Engl., 54, 10347-1035
Jaremko, L., Jaremko, M., Giller, K., Becker, S., Zweckstetter, M. (2015) Conformational flexibility in the transmembrane protein TSPO, Chem. Eur. J., 21, 16555-16563;
Jaremko, M., Jaremko, L., Mazur, A., Makowski, M., Lisowski, M. (2013) Enhanced β-turn conformational stability of tripeptides containing ΔPhe in cis over trans configuration, Amino Acids, 45, 865-875
Schwalbe, M., Ozenne, V., Bibow, S., Jaremko, M., Jaremko, L., Gajda, M., Ringkjøbing-Jensen, M., Biernat, J., Becker, S., Mandelkow, E., Zweckstetter, M., Blackledge, M. (2014) Predictive atomic resolution descriptions of intrinsically disordered hTau40 and α-synuclein in solution from NMR and small angle scattering, Structure, 22, 238-249
Jaremko, M., Jaremko, L., Kim, H.-Y., Cho, M.-K., Schwieters, C. D., Giller, K., Becker, S., Zweckstetter, M. (2013) Cold denaturation of a protein dimer monitored at atomic resolution, Nat. Chem. Biol., 9, 264-270