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.
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

Water exchange in magnesium’s hydration shells impacts biological processes

July 02, 2020

The dynamics of water exchange in the first hydration shell of magnesium are important to a variety of biological phenomena. Despite the importance, the microscopic mechanism of water exchange could not be resolved so far since it is out of reach for ...

A molecular view on protein retrotranslocation

April 27, 2020

Researchers at Harvard Medical School (USA), New York University School of Medicine (USA) and the Max Planck Institute of Biophysics developed a model of how misfolded proteins are recognised and retrotranslocated by the Hrd1 ubiquitin ligase complex ...

Enzyme catalysis by selective compression of bulky ring-shaped substrates

April 14, 2020

High-resolution crystal structures of tertiary methylene-tetrahydromethanopterin (H4MPT)-substrate complexes show how the substrates NADP+ and methylene-H4MPT are, at first, bound into an open catalytic cleft and then transferred into a strained but ...

The spikes of the virus crown

April 07, 2020

The spike glycoproteins give the coronavirus its name. The molecules protrude from the viral envelope like the spikes of a crown. Researchers at the Max Planck Institute of Biophysics in Frankfurt are now analysing the structure of this protein. They ...

Muscle cells need calcium ions

March 13, 2020

Wenbo Chen and Misha Kudryashev from the Max Planck Institute of Biophysics and the Buchmann Institute for Molecular Life Sciences of the Goethe University Frankfurt, have succeeded in elucidating the structure of RyR1 in closed and open states ...

Osmoregulation: Homeostasis is vital for bacteria

February 06, 2020

A research group led by Janet Vonck of the Max Planck Institute of Biophysics and Inga Hänelt of the Goethe University Frankfurt am Main examined the K+/H+ importer KimA, which belongs to the KUP family.

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