Max Planck Institute of Biophysics

Max Planck Institute 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. Scientists at the Institute use electron microscopes and X-rays to determine the spatial structure of these proteins. In addition, protein function is characterized by electrophysiology, a technique which measures the electric currents and voltages generated when electrically-charged atoms (ions) flow through membrane proteins. As an ideal complement to the experimental characterizations, these molecular processes are also studied theoretically to develop quantitative descriptions and to 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 no International Max Planck Research School (IMPRS).

There is always the possibility to do a PhD. Please contact the directors or research group leaders at the Institute.

ATP synthase: More ‘juice’ from black grapes
Researchers have developed a means of switching energy generation in cells on and off using UV light. more
Secretin protein with a crown
Researchers elucidate the structure of a molecular machine that allows bacteria to import foreign DNA and become resistant to antibiotics more
Structure of channelrhodopsin determined
Researchers discover structure and mechanism of action of molecular light switch, paving the way for new applications more
Information filter for immune defence
Researchers are deciphering the structure of the MHC-I peptide-loading complex. more
By using innovative labeling methods, Max Planck researchers develop a technique to measure newly synthesized proteins in the active mouse brain more

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.
No job offers available

Molecular mechanisms of lipid membrane shaping and quality control

2018 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. more

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

2017 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. more

How nature reduces molecular oxygen to water conserving energy at the same time

2016 Michel, Hartmut; Ermler, Ulrich; Safarian, Schara
Structural Biology
Molecular oxygen appeared in the atmosphere about three billion years ago. Nature developed two membrane integrated enzymatic systems which reduce oxygen to water and use the energy of this reaction to produce biologically important energy carriers. These enzymes are the haem-copper terminal oxidases, e.g. cytochrome c oxidase, and the bd oxidases. The atomic structures of representative members of both enzyme families were determined. These evolutionary unrelated enzymes apparently use the same mechanisms to conserve energy and to prevent the formation of toxic reactive oxygen species. more

Molecular Simulations: from biomolecular structures to function

2015 Hummer, Gerhard
Cell Biology Computer Science Evolutionary Biology Genetics Structural Biology
Molecular simulations allow us to study the functional mechanisms of biomolecules. Thanks to their enormously detailed description, by resolving the motion of every atom, such simulations help to interpret complex experiments. Simulations also allow us to venture into areas which are difficult to access by experiments, such as the detailed characterization of enzymatic reaction mechanisms. Moreover, by “watching proteins at work”, new and fundamental processes can be discovered by using molecular simulations. more

Current Research in Structural Biology

2014 Werner Kühlbrandt
Cell Biology Structural Biology
The Department elucidates the structure and function of membrane proteins as well as macromolecular protein complexes by using electron microscopy, x-ray crystallography, biochemical and biophysical methods. It consists of a group lead by director Werner Kühlbrandt and project groups operated by Janet Vonck and Özkan Yildiz. Thomas Meier and Daniel Rhinow run two independent research groups. Christine Ziegler, now appointed as professor at the University of Regensburg, is still associated with the Department. Here, we present current data and results from all over the Department’s research. more
Go to Editor View