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.
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

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 ...

Dynamic model of SARS-CoV-2 spike protein reveals potential new vaccine targets

April 01, 2021

A key feature of SARS-CoV-2 is its spike protein, which extends from its surface and enables it to target and infect human cells. Extensive research has resulted in detailed static models of the spike protein, but these models do not capture the ...

Structure of serotonin receptor in presence of lipids resolved

February 23, 2021

Once again, a step has been taken towards clarifying the action of the neurotransmitter serotonin, often referred to as the "happiness hormone", to one of its receptors, 5-HT3AR. An international team of researchers has succeeded now in elucidating ...

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PhD student (m/f/d) | MS-based proteomics

May 05, 2021
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