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.
With this award, the German National Academy of Sciences Leopoldina honours Werner Kühlbrandt, Director of the Department of Structural Biology, for his outstanding scientific lifetime achievement.

Werner Kühlbrandt receives the Cothenius Medal for his lifetime achievement

With this award, the German National Academy of Sciences Leopoldina honours Werner Kühlbrandt, Director of the Department of Structural Biology, for his outstanding scientific lifetime achievement.
This month, the renowned Science magazine published new results from Olivia Pfeil-Gardiner and Bonnie Murphy (Max Planck Insitut of Biophysics) in collaboration with researchers from the Max Planck Insitute for Terrestrial Microbiology, Marburg. New structures solved by the group shed light on direct and conformationally-controlled electron transfer for CO2 fixation in methanogens.

Murphy group’s work published in Science magazine: How methanogenic microbes manage electrons

This month, the renowned Science magazine published new results from Olivia Pfeil-Gardiner and Bonnie Murphy (Max Planck Insitut of Biophysics) in collaboration with researchers from the Max Planck Insitute for Terrestrial Microbiology, Marburg. New structures solved by the group shed light on direct and conformationally-controlled electron transfer for CO2 fixation in methanogens.
Our new graduate program International Max Planck Research School on Cellular Biophysics (IMPRS-CBP) welcomes its first PhD students and starts with an online symposium on Cellular Biophysics in October. Find the detailed program and the Zoom link on the IMPRS website.

IMPRS Symposium on Cellular Biophysics

Our new graduate program International Max Planck Research School on Cellular Biophysics (IMPRS-CBP) welcomes its first PhD students and starts with an online symposium on Cellular Biophysics in October. Find the detailed program and the Zoom link on the IMPRS website.
We are proud to announce that Melanie McDowell has been awarded a Max Planck Research Group Leader Position to start at our institute in February 2022. She aims to structurally characterise membrane protein biogenesis pathways at the endoplasmic reticulum. There will be open Postdoc, PhD and Technician positions. Click here for more information. 

Coming February 2022: New research group of Melanie McDowell

We are proud to announce that Melanie McDowell has been awarded a Max Planck Research Group Leader Position to start at our institute in February 2022. She aims to structurally characterise membrane protein biogenesis pathways at the endoplasmic reticulum. There will be open Postdoc, PhD and Technician positions. Click here for more information.

 
The MPI Biophysics has, together with GU Frankfurt, and JGU Mainz, launched its new International Max Planck Research School (IMPRS) on Cellular Biophysics. From now on, PhD students will join our school annually to pursue the school’s mission: to understand how complex subcellular architecture is created from individual molecular functions that act in concert. Further Information: www.imprs-cbp.mpg.de.

New “International Max Planck Research School on Cellular Biophysics” at our Institute

The MPI Biophysics has, together with GU Frankfurt, and JGU Mainz, launched its new International Max Planck Research School (IMPRS) on Cellular Biophysics. From now on, PhD students will join our school annually to pursue the school’s mission: to understand how complex subcellular architecture is created from individual molecular functions that act in concert. 
Further Information: www.imprs-cbp.mpg.de.
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

Wired for Efficiency: How methanogenic microbes manage electrons

September 02, 2021

Methanogenic archaea use sophisticated enzyme systems to live in energy-limited anoxic environments. A key mechanism for saving energy is electron bifurcation, a reaction that ‘splits’ the energy of a pair of electrons, making one more strongly ...

Enzyme structure supports microbial growth

July 15, 2021

Scientists at the Max Planck Institutes for Medical Research in Heidelberg, for Marine Microbiology in Bremen and for Biophysics in Frankfurt am Main, as well as the Radboud University in Nijmegen and other partners, have successfully determined the ...

An accurate atomistic description for the role of vital Magnesium in biological processes

April 08, 2021

Magnesium plays an essential role in many vital processes. To correctly describe its mode of action in biological systems by computer simulations, accurate models with atomistic resolution are crucial. Researchers in the group of Nadine Schwierz at ...

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