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Michael Senske is interested in the folding of proteins. © RUB, Marquard

RESOLV doctoral researcher awarded for work on protein stability

15 minutes – that was all the time Michael Senske had to impress the jury with his doctoral thesis. It was enough.

The Bochum-based doctoral candidate Michael Senske received an award for his doctoral thesis at a meeting of the Gesellschaft Deutscher Chemiker (GDCh - Association of German Chemists). Under the slogan “Thinking the unthinkable”, the association invited people to Berlin on 15th September 2017. The meeting was held to mark the 150thanniversary of the society and was part of the Scientific Forum Chemistry 2017. Besides expert talks by established professors, early career researchers were also given a chance to speak.

One of them was Michael Senske from the Institute of Laser Spectroscopy and Biophotonics at Ruhr-Universität Bochum. He presented results from his doctoral thesis in competition with other doctoral candidates. A total of three speakers had qualified for the presentations in a preselection. Senske represented the cluster of excellence RESOLV.

He won against the other competitors with his 15-minute talk. The jury honoured him with the award for best presentation by an early career chemist. Besides recognition of his academic work, Senske was even given a bonus. “There is also a small amount of prize money totalling 250 euros. I am delighted to receive this great award for my research results. The international collaboration between three research groups was certainly pivotal in this,” commented the lucky winner. 

Moleculeolecule origami: the folding of proteins

In his research, Senske looks at the stability of proteins. “If these are not folded in the right three-dimensional structure, they no longer fulfil their function in the cell. Illnesses such as Alzheimer’s or Huntington’s disease are most likely attributable to incorrectly folded proteins,” he explains.

Research into proteins is time-consuming. The researchers often make the work easier by isolating their target protein and examining it in small test tubes under laboratory conditions. But herein lies a problem, as Senske says: “The proteins’ environment can influence how they fold. In the living cell, they may have different properties than in a test solution in the lab.”

It is precisely these differences in protein folding that Senske investigated in his doctoral thesis. In doing so, he cooperated within the Resolv project with the working groups of Prof Dr Martina Havenith and Prof Dr Simon Ebbinghaus, as well as Prof Dr Gary Pielak from the University of North Carolina, Chapel Hill.


Original News on RUB website

Article: M. Senske et al. Angew Chem Int Ed Engl. 2016; 55:3586

Article: M. Senske et al. J. Am. Chem. Soc. 2014; 136:9036


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