RUHR EXPLORES SOLVATION SCIENCE

RUHR EXPLORES SOLVATION SCIENCE

We shape a new scientific discipline, inspire the scientists of tomorrow, and enable future technologies

WE ARE RESOLV

WE ARE RESOLV

Over 200 scientists from about 50 research groups in 7 institutions

ZEMOS: Home of Solvation Science @RUB

ZEMOS: Home of Solvation Science @RUB

The first research building for Solvation Science in the world. Hosts over 100 scientists, it's home to 6 disciplines.

WHAT is RESOLV?

The Cluster of Excellence RESOLV is an interdisciplinary research project of the Ruhr University Bochum and the TU Dortmund University, as well as four other institutions in the German Ruhr area. Since 2012, about 200 scientists cooperate to clarify how the solvent is involved in the control, mediation and regulation of chemical reactions. Our research is essential to advance technologies that could reuse CO2 for chemicals production, increase the efficiency of energy conversion and storage and develop smart sensors. RESOLV is funded by the German Federal Government and the state of North Rhine-Westphalia with 42 Mio. EUR over the period 2019-2025. 

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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.

Links:

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

Posted on
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.

Links:

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

Our scientific fields

Research Area A

Understanding and Exploiting Solvation in Chemical Processes

 

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Research Area B

Connecting Solvation Dynamics with Biomolecular Function

 

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Research Area C

Ion Solvation
and Charge Transfer at Interfaces

 

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Video: The solvent of life

Water. It’s the most abundant substance on Earth´s surface and in our bodies. But is water a passive spectator in the animated scene of bio-chemical reactions inside our cells? RESOLV scientists investigate the important role that water plays in the most diverse processes, bringing solvation science into the spotlight.

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Posted on
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.

Links:

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

gss summer school

The Graduate School Solvation Science hosts an annual Summer School at the Ruhr University Bochum. The school always takes place during Whitsuntide and is an integral part of the GSS students' training during their doctoral studies. This year's GSS Summer School took place from the 22nd to the 25th of May, 2018.

International speakers, suggested by the students themselves, are invited to give keynote talks on their research in the field of Solvation Science. The Advanced Laboratory Modules give the students an excellent opportunity to learn new and interesting experimental and theoretical techniques within a specific research topic of their own choice. 

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Publications highlight

K Lucht, D Loose, M Ruschmeier, V Strotkötter, G Dyker, K Morgenstern
Hydrophilicity and Microsolvation of an Organic Molecule Resolved on the Submolecular Level by Scanning Tunneling Microscopy, Angew. Chem. 57 (2018), 1266, DOI: 10.1002/anie.201711062

N Tsuji, JL Kennemur, T Buyck, S Lee, S Prévost, PSJ Kaib, D Bykov, C Farès, B List
Activation of olefins via asymmetric Brøsted acid, Science 359 (2018), 1501, DOI: 10.1126/science.aaq0445

D Muñoz-santiburcio, M Farnesi Camellone, D Marx
Solvation-Induced Changes in the Mechanism of Alcohol Oxidation at Gold/Titania Nanocatalysts in the Aqueous Phase versus Gas Phase, Angew. Chem. 57 (2018), 3327, DOI: 10.1002/anie.201710791

KF Pfister, S Baader, M Baader, S Berndt, LJ Goossen
Biofuel by isomerizing metathesis of rapeseed oil esters with (bio)ethylene for use in contemporary dieses engines, Science Advances  3 (2017),  e1602624, DOI: 10.1126/sciadv.1602624

C Schuabb, N Kumar, S Pataraia, D Marx, R Winter
Pressure modulates the self-cleavage step of the hairpin ribozyme, Nature Communications 8 (2017), 14661, DOI: 10.1038/ncomms14661

 

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