The International Max Planck Research School for Chemical and Molecular Biology (IMPRS-CMB) is a collaboration between the Max Planck Institute of Molecular Physiology and three universities, the Technical University Dortmund (TU Dortmund), the Ruhr University Bochum (RUB) and the University of Duisburg-Essen (DUE).

All four institutes are located in the Ruhr Metropolitan Area of Germany, an extremely vibrant and culturally interconnected region. The same spirit is reflected in the science of our program: research groups, with different and often complementary approaches, combine their efforts to study at the molecular level basic cell physiology.

Below you can find all the research groups that are part of IMPRS-CMB, in alphabetical order. You can also search groups by name, topic or technique.

Read about OUR SCIENCE by visiting the webpages of our Faculty Members.


Prof. Dr. Roland Winter

Since 1993: Chair of Physical Chemistry I (Biophysical Chemistry) at TU Dortmund University
1992-1993: Professor of Physical Chemistry, Dept. of Chemistry, Ruhr-University Bochum
1991: Habilitation and Venia Legendi in Physical Chemistry, Philipps-University Marburg
1987-1988: Visiting Scientist, Dept. of Chemistry, University of Illinois at Urbana-Champaign, USA
1982: Ph.D. (Dr. rer. nat.), University (TH) of Karlsruhe
1979: Diploma in Chemistry, University (TH) of Karlsruhe

Research Interest
The structure, dynamics and phase behavior of model biomembranes and proteins, and the kinetics of biomolecular transformations is studied. Our emphasis in the field of membrane biophysics is the study of the energetics and phase behavior of lipid mesophases, the interaction of model biomembranes with polypeptides, and in particular of membrane-associated signaling processes. We also address pressure effects in molecular biophysics, such as pressure-induced phase transformations of lipid membranes, and unfolding, denaturation and aggregation (amyloidogenesis) processes of proteins. Besides the general physical-chemical interest in using high pressure as a tool for understanding the structure, energetics and conformational dynamics of biomolecules, high pressure is also of considerable physiological and biotechnological interest.

X-ray and neutron scattering, calorimetry, surface plasmon resonance, CD-, FTIR-, fluorescence and NMR spectroscopy, infrared reflection absorption spectroscopy (IRRAS), AFM and fluorescence microscopy, stopped-flow kinetics, high pressure techniques.

Selected Reading
Möller J, Grobelny S, Schulze J, Bieder S, Steffen A, Erlkamp M, Paulus M, Tolan M, Winter R. Reentrant liquid-liquid phase separation in protein solutions at elevated hydrostatic pressures. Phys Rev Lett 2014, 112(2), 028101.

Kapoor S, Werkmüller A, Goody RS, Waldmann H, Winter R. Pressure modulation of Ras-membrane interactions and intervesicle transfer. J Am Chem Soc 2013, 135(16), 6149-6156.

Kapoor S, Triola G, Vetter IR, Erlkamp M, Waldmann H, Winter R. Revealing conformational substates of lipidated N-Ras protein by pressure modulation. Proc Natl Acad Sci USA 2012, 109(2), 460-465.

Seeliger J, Evers F, Jeworrek C, Kapoor S, Weise K, Andreetto E, Tolan M, Kapurniotu A, Winter R. Cross-amyloid interaction of Aβ and IAPP at lipid membranes. Angew Chem Int Ed 2012, 51(3), 679-683.

Weise K, Kapoor S, Denter C, Nikolaus J, Opitz N, Koch S, Triola G, Herrmann A, Waldmann H, Winter R. Membrane-mediated induction and sorting of K-Ras microdomain signaling platforms. J Am Chem Soc 2011, 133, 880-887.

Mishra R and Winter R. Cold- and pressure-induced dissociation of protein aggregates and amyloid fibrils. Angew Chem Int Ed 2008, 47, 6518-6521.

Daniel I, Oger P, Winter R. Origins of life and biochemistry under high-pressure conditions. Chem Soc Rev 2006, 35, 858-875.


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