The Max Planck Institute of Biophysics focuses on investigating the structure and function of proteins that are embedded in cellular membranes. Membrane proteins functioning as channels, transporters, or molecular sensors mediate the exchange of matter and information of cells with their environment.

Welcome to the MPI of Biophysics!

The Max Planck Institute of Biophysics focuses on investigating the structure and function of proteins that are embedded in cellular membranes. Membrane proteins functioning as channels, transporters, or molecular sensors mediate the exchange of matter and information of cells with their environment.
Beata Turoňová et al. In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges Science, 18 August 2020

New findings on SARS-CoV-2 protein shed light on virus’ ability to infect cells

Beata Turoňová et al. In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges Science, 18 August 2020
Reduction of molecular oxygen to water is the driving force for respiration in aerobic organisms and is catalyzed by several distinct integral membrane complexes. These include an exclusively prokaryotic enzyme, cytochrome bd–type quinol oxidase, which is a potential antimicrobial target. Safarian, Hahn et al. determined a high-resolution cryo–electron microscopy structure of this enzyme from the enteric bacterium Escherichia coli.

Active site rearrangement and structural divergence in prokaryotic respiratory oxidases

Reduction of molecular oxygen to water is the driving force for respiration in aerobic organisms and is catalyzed by several distinct integral membrane complexes. These include an exclusively prokaryotic enzyme, cytochrome bd–type quinol oxidase, which is a potential antimicrobial target. Safarian, Hahn et al. determined a high-resolution cryo–electron microscopy structure of this enzyme from the enteric bacterium Escherichia coli.
Hampoelz B., Schwarz A., et al., Cell 2019The molecular events that direct nuclear pore complex (NPC) assembly toward nuclear envelopes have been conceptualized in two pathways that occur during mitosis or interphase.

Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.

Hampoelz B., Schwarz A., et al., Cell 2019
The molecular events that direct nuclear pore complex (NPC) assembly toward nuclear envelopes have been conceptualized in two pathways that occur during mitosis or interphase.
Murphy, B., Klusch, N. et al., Science (2019) The authors solved high-resolution cryo–electron microscopy structures of the ATP synthase complex, extracting 13 rotational substates. This collection of structures revealed that the rotation of the Fo ring and central stalk is coupled with partial rotations of the F1 head. 

Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling

Murphy, B., Klusch, N. et al., Science (2019)
The authors solved high-resolution cryo–electron microscopy structures of the ATP synthase complex, extracting 13 rotational substates. This collection of structures revealed that the rotation of the Fo ring and central stalk is coupled with partial rotations of the F1 head. 
Turoňová, B., et al., Nature Communications (2020) The authors find that although any of the prominently used acquisition schemes is sufficient to obtain subnanometer resolution, dose-symmetric acquisition provides considerably better outcome. 

Benchmarking tomographic acquisition schemes for high-resolution structural biology

Turoňová, B., et al., Nature Communications (2020)
The authors find that although any of the prominently used acquisition schemes is sufficient to obtain subnanometer resolution, dose-symmetric acquisition provides considerably better outcome. 
Bhaskara, R.M., et al., Nature Communications (2019) Using molecular modeling and molecular dynamics (MD) simulations, the authors assemble a structural model for the RHD of FAM134B. 

Curvature induction and membrane remodeling by FAM134B reticulon homology domain assist selective ER-phagy.

Bhaskara, R.M., et al., Nature Communications (2019)
Using molecular modeling and molecular dynamics (MD) simulations, the authors assemble a structural model for the RHD of FAM134B. 

Latest News & Research

Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.

Hampoelz, Schwarz, et al., Cell 2019

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Rotary substates of mitochondrial ATP synthase

Murphy, B., Klusch, N. et al., Science (2019)

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Upcoming Events

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Welcome: Murphy Lab

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The spikes of the virus crown - Corona Research @MPI-BP

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We have a new grant office!

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New Department: Molecular Sociology

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Ernst Bamberg receives the Rumford Prize

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Our Research

Martin Beck

Research in this group combines biochemical approaches, proteomics and cryo-electron microscopy to study large macromolecular assemblies.

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Ulrich Ermler

Our major biological interest is directed to enzymes catalyzing biological degradation processes such as the methanogenic pathway.

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Gerhard Hummer

Our goal is to develop detailed and quantitative descriptions of key biomolecular processes.

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Misha Kudryashev

We use single particle cryo-EM to gain insights into gating and regulation of these important molecules.

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Werner Kühlbrandt

Our goal is to understand the structure and function of membrane proteins and large membrane protein complexes.

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Julian Langer

The “Proteomics and membrane mass spectrometry” lab is funded by the MPIs for Biophysics and Brain Research.

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Hartmut Michel

We determine structure and mechanism of action using membrane proteins from cellular respiration and photosynthesis.

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Bonnie Murphy

We use single-particle cryo-EM to better understand the structure and function of proteins central to bioenergetics.

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Nadine Schwierz

We address theoretical description of biological soft matter systems using statistical physics and computer simulations.

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Sonja Welsch

Applying and advancing state-of-the-art electron microscopy techniques to deepen our understanding of biological systems.

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Latest Press Releases

Study unravels details of autophagy machinery assembly

September 07, 2020

Researchers from the University of Vienna, the Max Planck Institute for Biology of Ageing in Cologne and the Max Planck Institute of Biophysics in Frankfurt am Main succeeded in the reconstitution of the autophagosome nucleation using recombinant ...

Nuclear pores in their natural context

September 02, 2020

Scientists from the Max Planck Institutes of Biophysics and Biochemistry and the European Molecular Biology Laboratory, led by Boris Pfander, Jan Kosinski und Martin Beck have studied the 3D structure of nuclear pores in budding yeast (Saccharomyces ...

Flexible and protected – New findings on SARS-CoV-2 protein shed light on virus’ ability to infect cells.

August 18, 2020

In the fight against the coronavirus SARS-CoV-2 researchers from various research institutions in Germany joined forces to study the spike protein on the surface of the virus – this protein allows the virus to bind to and to infect human cells. The ...

COVID-19 research: Anti-viral strategy with double effect

July 29, 2020

When the SARS-CoV-2 virus penetrates human cells, it lets the human host cell produce proteins for it. One of these viral proteins, called PLpro, is essential for the replication and rapid spread of the virus. An international team of researchers led ...

A new approach for higher resolution structure determination of macromolecules in their native context

July 27, 2020

Cryo-electron tomography that was combined with subtomogram averaging (StA) has yielded high-resolution structures of macromolecules in their native context. However, high-resolution StA is not commonplace due to beam-induced sample drift, images ...

How smart, ultrathin nanosheets go fishing for proteins

July 20, 2020

An interdisciplinary team from Frankfurt am Main and Jena has developed a kind of bait with which to fish protein complexes out of mixtures. Thanks to this “bait”, the desired protein is available much faster for further examination in the electron ...

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