Max Planck Institute of Biophysics

Max Planck Institute of Biophysics

At the Max Planck Institute of Biophysics, research is mainly focused on proteins that are embedded in or associated with biological membranes. Among other things, membrane proteins act as channels, transporters or molecular sensors for the exchange of substances and information between the cell and its environment, but they are also important for transport within cells. The Institute's scientists use electron microscopy and X-ray crystallography to analyse the structure of these proteins. In an ideal complement to the experimental investigations, these molecular processes are also modelled in the computer, in order to describe them quantitatively and gain a detailed understanding of the underlying mechanisms.


Max-von-Laue-Straße 3
60438 Frankfurt am Main
Phone: +49 69 6303-0
Fax: +49 69 6303-4502

PhD opportunities

This institute has an International Max Planck Research School (IMPRS):

IMPRS on Cellular Biophysics

In addition, there is the possibility of individual doctoral research. Please contact the directors or research group leaders at the Institute.

Claire Donnelly and Eugene Kim receive the 2024 Heinz Maier-Leibnitz Prize of the German Research Foundation

Claire Donnelly and Eugene Kim will receive the 2024 Heinz Maier-Leibnitz Prize of the German Research Foundation

Model of the sugar shield (green) on the GABAA receptor (grey) in a membrane (red) generated by GlycoSHIELD.

Researchers develop novel method to predict the morphology of sugar coats on clinically relevant proteins within minutes


Scientists reveal how phosphate escapes from actin filaments


Illustration on the cover of the Journal Nature Chemical Biology underlines importance of the discovery

Bonnie J. Murphy from the Max Planck Institute of Biophysics in Frankfurt/Main, and Giulio Malavolta from the Max Planck Institute for Security and Privacy in Bochum, who receive the Heinz Maier-Leibnitz Prize 2023 for their research.

The German Research Foundation recognizes Bonnie J. Murphy and Giulio Malavolta with the Heinz Maier-Leibnitz Prize

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Talking with friends, enjoying a concert, talking on the phone on noisy streets – people with hearing problems are often unable to hear things that others can. Tobias Moser aims to make sound accessible to those with hearing disabilities in a whole new way through a new generation of hearing protheses. Known as optical cochlear implants, these devices serve as an example of therapies developed on the basis of fundamental research.

Custom-Tailored Molecules

4/2014 Biology & Medicine

Chlamydomonas reinhardtii, a single-celled green alga, can’t see much at all with its eye composed solely of photosensitive rhodopsin molecules. Yet there is more to algal rhodopsin than one would expect. In recent years, it has triggered a revolution in neurobiology. Ernst Bamberg from the Max Planck Institute of Biophysics in Frankfurt helped make it famous. He is now researching these molecules and developing new variants for basic research and medical applications.

Coordinator (m/f/d) of the Graduate Program

Max Planck Institute of Biophysics, Frankfurt am Main May 02, 2024

The mind-boggling jigsaw puzzle of the nuclear pores 

2022 Beck, Martin; Hummer, Gerhard

Cell Biology Genetics Structural Biology

As control units of our cells, nuclei contain and guard our genetic material. Pores in the nuclear membrane form the only gateway in and out of the nucleus, allowing important messenger molecules to pass but blocking dangerous invaders such as pathogens. They thus help the nucleus to communicate with the rest of the cell while protecting the genetic material. Such challenging task requires a complex biological structure that has kept many scientists occupied for over two decades; a jigsaw puzzle with missing pieces that we could now solve to near completion.


Electron cryo-microscopy of membrane protein complexes

2019 Kühlbrandt, Werner

Structural Biology

Single-particle electron cryo-microscopy (CryoEM) is ideal for determining the high-resolution structure membrane protein complexes that are too unstable or too dynamic for x-ray crystallography. Intact rotary ATPases have resisted crystallization for more than 40 years. However, central aspects of their mechanisms now have become clear thanks to the recent CryoEM based structures of intact, functional ATP synthases. The two best and most informative of these structures, the chloroplast ATP synthase and a mitochondrial ATP synthase dimer, have been shown by our department.


Acyl-CoA dehydrogenase/electron-transferring flavoprotein complexes: Structural determinants of a flavin-based electron bifurcation

2018 Kayastha, Kanwal; Demmer, Julius K.; Müller, Volker; Buckel, Wolfgang; Ermler, Ulrich

Cell Biology

Flavin-based electron bifurcating (FBEB) enzyme complexes play a vital role in obligate anaerobic microorganisms for increasing the efficiency of their energy metabolism. They drive an endergonic reduction by an exergonic one via the same electron donor. The energy coupling is realized by a reduced flavin which transfers via energy splitting one strongly and one weakly reducing electron to two different substrates. How FBEB enzyme complexes are structurally constructed is outlined using the example of two acyl-CoA dehydrogenase/electron-transferring flavoproteins.


Molecular mechanisms of lipid membrane shaping and quality control

2017 Hummer, Gerhard

Cell Biology Structural Biology

Living cells are coated and structured by lipid membranes. We addressed two important questions: how are membranes shaped into their often unusual forms, and how do cells monitor the membrane state? With molecular and coarse-grained simulations, we could show how the proteins Mga2 and Ire1 can sense the state of the endoplasmic reticulum. Also, new insights have been obtained about the fusion of vesicles, the formation of tubular structures in the endoplasmic reticulum, and the induction of autophagosomes aided by the Atg1 complex.


Structure of dimeric ATP synthase from the inner membrane of yeast mitochondria

2016 Hahn, Alexander; Parey, Kristian; Bublitz, Maike; Mills, Deryck J.; Zickermann, Volker; Vonck, Janet; Kühlbrandt, Werner; Meier, Thomas

Cell Biology Structural Biology

We determined the structure of a complete, dimeric F1Fo-ATP synthase from mitochondria of the yeast Yarrowia lipolytica by a combination of cryo-electron microscopy (cryo-EM) and X-ray crystallography. The structure resolves 58 of the 60 subunits in the dimer. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Our data explain the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology.

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