WE ARE RESOLV

Over 200 scientists from about 50 research groups in 6 institutions

RUHR EXPLORES SOLVATION

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

Diversity, Equity, and Inclusion (DEI) in Science Day

Equity and diversity as a source of strength, fundamental to innovative ideas, and a prerequisite for excellence in science

Summer School Solvation Science

We are happy to welcome young Solvation Scientists every year after Whitsun in Bochum

World Science Day

Building strong networks between academia and industry

ZEMOS: Home of Solvation Science

The first research building for Solvation Science in the world @ Ruhr University Bochum

CALEDO: Research Building for Solvation Science

Center for Advanced Liquid-Phase Engineering @TU Dortmund University

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, develop smart sensors, or enhance drug delivery. Over its third funding period (2026-2032), RESOLV is supported by the German Federal Government and the State of North Rhine-Westphalia with 43 Mio. Euro.

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Video: THIS is RESOLV

RESOLV pioneered Solvation Science as an interdisciplinary research field. It has transformed its host universities into excellent research ecosystems and embedded researchers at all stages of their careers in an international network of scientists.

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Posted on 07/21/2026

Prof. Simon Ebbinghaus and Mailin Becker © Chair of Biophysical Chemistry

Researchers compare protein folding within cells

PRX Life: A group of researchers including RESOLV member Prof. Simon Ebbinghaus has developed a new method that makes it possible to measure the stability of proteins at various points within an individual cell.

This sheds more light on the development of neurodegenerative diseases.

Protein aggregates are associated with the development of diseases like Alzheimer’s and Parkinson’s. These are found more often in certain areas of cells known as membraneless organelles. Do these organelles promote this protein clumping, or do they protect the cell by temporarily absorbing the aggregates? Professor Simon Ebbinghaus and Mailin Becker from Ruhr University Bochum, Germany, set out to answer this question with their new, self-developed method “confocal Fast Relaxation Imaging,” or cFReI.

They reported their findings recently in the journal PRX Life.

RUB press release

Original publication

Overview

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Posted on 07/21/2026

Researchers compare protein folding within cells

PRX Life: A group of researchers including RESOLV member Prof. Simon Ebbinghaus has developed a new method that makes it possible to measure the stability of proteins at various points within an individual cell.

This sheds more light on the development of neurodegenerative diseases.

Protein aggregates are associated with the development of diseases like Alzheimer’s and Parkinson’s. These are found more often in certain areas of cells known as membraneless organelles. Do these organelles promote this protein clumping, or do they protect the cell by temporarily absorbing the aggregates? Professor Simon Ebbinghaus and Mailin Becker from Ruhr University Bochum, Germany, set out to answer this question with their new, self-developed method “confocal Fast Relaxation Imaging,” or cFReI.

They reported their findings recently in the journal PRX Life.

RUB press release

Original publication

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@SolvationSci

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Cluster of Excellence RESOLV

Our scientific fields

Research Area I

Charge and Electron Transfer

Research Area II

Solvent Design for Chemical Processes

Research Area III

Tuning Stability and Homogeneity

Upcoming Events or browse all

Overview

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Posted on 07/21/2026

Researchers compare protein folding within cells

PRX Life: A group of researchers including RESOLV member Prof. Simon Ebbinghaus has developed a new method that makes it possible to measure the stability of proteins at various points within an individual cell.

This sheds more light on the development of neurodegenerative diseases.

Protein aggregates are associated with the development of diseases like Alzheimer’s and Parkinson’s. These are found more often in certain areas of cells known as membraneless organelles. Do these organelles promote this protein clumping, or do they protect the cell by temporarily absorbing the aggregates? Professor Simon Ebbinghaus and Mailin Becker from Ruhr University Bochum, Germany, set out to answer this question with their new, self-developed method “confocal Fast Relaxation Imaging,” or cFReI.

They reported their findings recently in the journal PRX Life.

RUB press release

Original publication

Summer School Solvation Science

RESOLV hosts an annual summer school at ZEMOS, Ruhr University Bochum. The school always takes place after Whitsun and is an integral part of the integrated Graduate School Solvation Science (iGSS) students' training during their doctoral studies. Scholarships for international students and PhD candidates are also available upon admission.

International speakers, suggested by a committee of iGSS students and RESOLV postdocs, are invited to give keynote talks on their research in the field of Solvation Science. In career-boosting workshops, summer school participants may meet industry professionals or fine-tune their personal skills. The Advanced Laboratory Modules offer 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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Publication highlights

G. A. Virgen, S. Skoko, A. M. Stingel, T. Goswami, R. L. Cole, D. C. Crans, P. B. Petersen, A. Vila Verde, N. E. Levinger, Proc. Natl. Acad. Sci. U.S.A 123, e2518988123 (2026), 10.1073/pnas.2518988123

T. Kistwal, K. Kanhaiya, A. Buchmann, C. Ma, J. Nikolić, J. Ackermann, P. Galonska, S. S. Nalige, V. Sardari, A. Sudarsan, M. Havenith, M. Sulpizi, S. Kruss, Light-induced quantum friction of carbon nanotubes in water, Nature UK (2026), 10.1038/s41586-026-10632-2

W. Chen, M. Gruebele, M. Havenith, K. J. Hebel, C. Scaletti, Water-mediated Hydrogen Bonds and Local Side Chain Interactions in the Cooperative Collapse and Expansion of PNIPAM Oligomers, Proc. Natl. Acad. Sci. U.S.A 123, e2523755123 (2026), 10.1073/pnas.2523755123

Y. Cao, J. Mieres-Perez, J. F. Rowen, A. H. Raut, P. Schweer, A. Bao, W. Sander, E. Sánchez-García, K. Morgenstern, On-surface synthesis platform for highly branched oligomers based on sequential C–C coupling and C–H activation of carbenes, Nat. Commun. 17, 1145 (2025), 10.1038/s41467-025-67604-9

T. Tabassum, B. Das, C. Park, S. Ghosh, D. Naujoks, S. M. Piontek, A. Ludwig, D. Marx, P. B. Petersen, Hydrophobic versus Hydrophilic Nature of the Gold-Water Interface Determined by Fluctuating Local Water Orientation, Phys. Rev. Lett. 135, (2025), 116201, 10.1103/7ht1-xv82

S. Ghosh, C. K. Das, S. Uddin, S. T. Stripp, V. Engelbrecht, M. Winkler, S. Leimkuhler, C. Brocks, J. Duan, L. V. Schäfer, T. Happe, Protein Dynamics Affect O2-Stability of Group B [FeFe]-Hydrogenase from Thermosediminibacter oceani, J. Am. Chem. Soc. 147, 15170-15180 (2025). 10.1021/jacs.4c18483

D. L. Reinhard, A. Iniutina, S. Reese, T. Shaw, C. Merten, B. List, S. M. Huber, Asymmetric Counteranion-Directed Halogen Bonding Catalysis, J. Am. Chem. Soc. 147, 8107-8112 (2025). 10.1021/jacs.4c18378

K. E. Ebbert, F. Sendzik, L. Neukirch, L. Eberlein, A. Platzek, P. Kibies, S. M. Kast, G. H. Clever, Solvent-Controlled Separation of Integratively Self-Sorted Pd2LA2LB2 Coordination Cages, Angew. Chem. Int. Ed. 64, e202416076 (2025), 10.1002/anie.202416076

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